TY  - CONF
AU  - Pantelić, Ana
AU  - Prodić, Ivana
AU  - Milić, Dejana
AU  - Senćanski, Milan
AU  - Vidović, Marija
PY  - 2023
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2149
AB  - Introduction: Resurrection plants (such as Ramonda serbica) can survive a long desiccation period and
fully resume their metabolism upon watering. The hallmark of desiccation tolerance (DT) is the accumulation of protective, intrinsically disordered proteins(IDPs), called late embryogenesis abundant proteins (LEAPs). Although their high structural plasticity allows them to interact with various partners, no
specific cellular targets of LEAPs have been identified so far.
Methods: To identify LEAPsinvolved in DT, differential transcriptome and proteome analyses of hydrated
and desiccated R. serbica leaves were performed. The identified LEAPs were structurally characterised
and classified. To evaluate theirstructural propertiesin vitro and their potential functionsin vivo, the representative RsLEA proteins, were produced in Escherichia coli using recombinant DNA technology.
Results: Members of the LEA4 protein family represent the majority of desiccation-inducible LEAPs. Even
17 proteins belonging to the LEA4 protein family group were induced by desiccation. They show high disorder propensity (82 %), and at the same time, a high tendency to form α-helices (>80%). Although recombinant DNA technology has traditionally been used to overexpress and purify various globular
proteins, the production of IDPsis challenging due to their high susceptibility to proteolytic cleavage and
aggregation. Nevertheless, the representative LEAPs containing hexa-Histagsimmunoglobulin G-binding protein and a proteolytic TEV site were produced, purified and cleaved by TEV protease.
Conclusion: The combination of in silico and in vitro results will be crucial for the identification of endogenous partners of LEAPs, providing further insight into their role in DT.
PB  - Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade
C3  - CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
T1  - Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica
EP  - 110
SP  - 110
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2149
ER  - 

@conference{
author = "Pantelić, Ana and Prodić, Ivana and Milić, Dejana and Senćanski, Milan and Vidović, Marija",
year = "2023",
abstract = "Introduction: Resurrection plants (such as Ramonda serbica) can survive a long desiccation period and
fully resume their metabolism upon watering. The hallmark of desiccation tolerance (DT) is the accumulation of protective, intrinsically disordered proteins(IDPs), called late embryogenesis abundant proteins (LEAPs). Although their high structural plasticity allows them to interact with various partners, no
specific cellular targets of LEAPs have been identified so far.
Methods: To identify LEAPsinvolved in DT, differential transcriptome and proteome analyses of hydrated
and desiccated R. serbica leaves were performed. The identified LEAPs were structurally characterised
and classified. To evaluate theirstructural propertiesin vitro and their potential functionsin vivo, the representative RsLEA proteins, were produced in Escherichia coli using recombinant DNA technology.
Results: Members of the LEA4 protein family represent the majority of desiccation-inducible LEAPs. Even
17 proteins belonging to the LEA4 protein family group were induced by desiccation. They show high disorder propensity (82 %), and at the same time, a high tendency to form α-helices (>80%). Although recombinant DNA technology has traditionally been used to overexpress and purify various globular
proteins, the production of IDPsis challenging due to their high susceptibility to proteolytic cleavage and
aggregation. Nevertheless, the representative LEAPs containing hexa-Histagsimmunoglobulin G-binding protein and a proteolytic TEV site were produced, purified and cleaved by TEV protease.
Conclusion: The combination of in silico and in vitro results will be crucial for the identification of endogenous partners of LEAPs, providing further insight into their role in DT.",
publisher = "Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade",
journal = "CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia",
title = "Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica",
pages = "110-110",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2149"
}

Pantelić, A., Prodić, I., Milić, D., Senćanski, M.,& Vidović, M.. (2023). Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade., 110-110.
https://hdl.handle.net/21.15107/rcub_imagine_2149

Pantelić A, Prodić I, Milić D, Senćanski M, Vidović M. Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia. 2023;:110-110.
https://hdl.handle.net/21.15107/rcub_imagine_2149 .

Pantelić, Ana, Prodić, Ivana, Milić, Dejana, Senćanski, Milan, Vidović, Marija, "Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica" in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia (2023):110-110,
https://hdl.handle.net/21.15107/rcub_imagine_2149 .

TY  - CONF
AU  - Vidović, Marija
AU  - Battisti, Ilaria
AU  - Pantelić, Ana
AU  - Milić, Dejana
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović Jovanović, Sonja
PY  - 2023
UR  - https://belbi.bg.ac.rs/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2005
AB  - The resurrection plant Ramonda serbica Panc. survives long desiccation periods and fully
recovers metabolic functions within one day upon watering. We aimed to identify key
candidates and pathways involved in desiccation tolerance in R. serbica by employing a
systems biology approach, combining transcriptomics and proteomics.
A total of 68,694 differentially expressed genes (DEGs; p-value<0.005 and abs(log2FC)≥2) were
obtained in R. serbica leaves upon desiccation. Among them, 23,935 and 26,169 genes were
upregulated and downregulated in desiccated leaves (DL) and hydrated leaves (HL), respectively.
By differential TMT-based proteomic analysis 1192 different protein groups were identified
after filtering with at least two unique peptides per protein. In total, 229 protein groups
were more abundant in HL and 179 in DL (p-value<0.05 and abs(FC)≥1.3). The majority
of the DAPs and DEGs involved in photosynthesis, transport, secondary metabolism, and
signaling, were less abundant in DL. On the other hand, proteins and transcripts associated
with fermentation, N-metabolism, heme, protein synthesis, folding and assembly, C1-
metabolism, and late embryogenesis abundant proteins, were more accumulated in DL.
A poor correlation between proteomic and transcriptomic results was detected for mitochondrial
electron transport and ATP production, gluconeogenesis, glycolysis, tricarboxylic
acid cycle, and enzymatic H2O2 scavengers due to different mRNA half-life, protein turnover,
dynamic posttranscriptional and posttranslational modifications. Finally, desiccation tolerance
in R. serbica is a species-specific process orchestrated by several metabolic pathways
that are temporally and compartmentally regulated at several levels.
PB  - Belgrade : Institute of molecular genetics and genetic engineering
C3  - 4th Belgrade Bioinformatics Conference
T1  - Integration of differential transcriptomic and proteomic data in hydrated and desiccated leaves of Ramonda serbica Panc.
EP  - 65
SP  - 65
VL  - 4
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2005
ER  - 

@conference{
author = "Vidović, Marija and Battisti, Ilaria and Pantelić, Ana and Milić, Dejana and Arrigoni, Giorgio and Masi, Antonio and Veljović Jovanović, Sonja",
year = "2023",
abstract = "The resurrection plant Ramonda serbica Panc. survives long desiccation periods and fully
recovers metabolic functions within one day upon watering. We aimed to identify key
candidates and pathways involved in desiccation tolerance in R. serbica by employing a
systems biology approach, combining transcriptomics and proteomics.
A total of 68,694 differentially expressed genes (DEGs; p-value<0.005 and abs(log2FC)≥2) were
obtained in R. serbica leaves upon desiccation. Among them, 23,935 and 26,169 genes were
upregulated and downregulated in desiccated leaves (DL) and hydrated leaves (HL), respectively.
By differential TMT-based proteomic analysis 1192 different protein groups were identified
after filtering with at least two unique peptides per protein. In total, 229 protein groups
were more abundant in HL and 179 in DL (p-value<0.05 and abs(FC)≥1.3). The majority
of the DAPs and DEGs involved in photosynthesis, transport, secondary metabolism, and
signaling, were less abundant in DL. On the other hand, proteins and transcripts associated
with fermentation, N-metabolism, heme, protein synthesis, folding and assembly, C1-
metabolism, and late embryogenesis abundant proteins, were more accumulated in DL.
A poor correlation between proteomic and transcriptomic results was detected for mitochondrial
electron transport and ATP production, gluconeogenesis, glycolysis, tricarboxylic
acid cycle, and enzymatic H2O2 scavengers due to different mRNA half-life, protein turnover,
dynamic posttranscriptional and posttranslational modifications. Finally, desiccation tolerance
in R. serbica is a species-specific process orchestrated by several metabolic pathways
that are temporally and compartmentally regulated at several levels.",
publisher = "Belgrade : Institute of molecular genetics and genetic engineering",
journal = "4th Belgrade Bioinformatics Conference",
title = "Integration of differential transcriptomic and proteomic data in hydrated and desiccated leaves of Ramonda serbica Panc.",
pages = "65-65",
volume = "4",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2005"
}

Vidović, M., Battisti, I., Pantelić, A., Milić, D., Arrigoni, G., Masi, A.,& Veljović Jovanović, S.. (2023). Integration of differential transcriptomic and proteomic data in hydrated and desiccated leaves of Ramonda serbica Panc.. in 4th Belgrade Bioinformatics Conference
Belgrade : Institute of molecular genetics and genetic engineering., 4, 65-65.
https://hdl.handle.net/21.15107/rcub_imagine_2005

Vidović M, Battisti I, Pantelić A, Milić D, Arrigoni G, Masi A, Veljović Jovanović S. Integration of differential transcriptomic and proteomic data in hydrated and desiccated leaves of Ramonda serbica Panc.. in 4th Belgrade Bioinformatics Conference. 2023;4:65-65.
https://hdl.handle.net/21.15107/rcub_imagine_2005 .

Vidović, Marija, Battisti, Ilaria, Pantelić, Ana, Milić, Dejana, Arrigoni, Giorgio, Masi, Antonio, Veljović Jovanović, Sonja, "Integration of differential transcriptomic and proteomic data in hydrated and desiccated leaves of Ramonda serbica Panc." in 4th Belgrade Bioinformatics Conference, 4 (2023):65-65,
https://hdl.handle.net/21.15107/rcub_imagine_2005 .

TY  - CONF
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
AU  - Milić Komić, Sonja
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2023
UR  - https://belbi.bg.ac.rs/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2008
AB  - Ramonda serbica Panc. is an ancient resurrection plant, that survives a long desiccation period
and fully recovers metabolic functions upon watering. The main characteristic of desiccationtolerant
plant species is their ability to accumulate protective late embryogenesis abounded
protein (LEAPs). To propose their role in R. serbica desiccation tolerance we structurally
analysed LEAPs in hydrated and desiccated leaves.
According to transcriptomics, 318 LEAPs were identified and classified into seven family
groups based on protein BLAST analysis and conserved motifs (Pfam). The largest LEAPs
belonged to the LEA2 and LEA4 protein family groups. We employed online tools to analyse
physicochemical characteristics (Expasy, ProtParam, BioPython, GRAVY calculator), disorder
propensity, and characterization protein structures (FELLS, JPred, SOPMA, PsiPred, Phyre2,
Espritz-DisProt, Espritz-X, Iupred, TMHMM, +Heliquest).
The most abundant, atypical LEA2 group containing 127, mostly hydrophobic proteins, was
divided into five subgroups. Members of this group were predicted to fold into globular
domains, β-barrel at the C-terminus, followed by transmembrane hydrophobic-helices and
disordered N-terminal regions. Results indicated the possible involvement in the protection
of the chloroplastic membranes.
The LEA4 group exhibited an exceptionally high tendency to form amphipathic α-helices and
simultaneously had a high disorder propensity. This group is made of 96 proteins, classified into 3
subgroups. The high content of polar and charged amino acids (lysine, glutamate, and aspartate) is
characteristic of this group. Motifs corresponding to the R. serbica LEA4 protein family group folded
into A-type α-helices that contained positive, negative, and hydrophobic surfaces. Based on previous
knowledge, the possible functions of the LEA2 and LEA4 groups are discussed with significant
implications on cell preservation technology and the improvement of crop drought tolerance.
PB  - Belgrade : Institute of molecular genetics and genetic engineering
C3  - 4th Belgrade Bioinformatics Conference
T1  - Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.
EP  - 68
SP  - 68
VL  - 4
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2008
ER  - 

@conference{
author = "Pantelić, Ana and Stevanović, Strahinja and Milić Komić, Sonja and Kilibarda, Nataša and Vidović, Marija",
year = "2023",
abstract = "Ramonda serbica Panc. is an ancient resurrection plant, that survives a long desiccation period
and fully recovers metabolic functions upon watering. The main characteristic of desiccationtolerant
plant species is their ability to accumulate protective late embryogenesis abounded
protein (LEAPs). To propose their role in R. serbica desiccation tolerance we structurally
analysed LEAPs in hydrated and desiccated leaves.
According to transcriptomics, 318 LEAPs were identified and classified into seven family
groups based on protein BLAST analysis and conserved motifs (Pfam). The largest LEAPs
belonged to the LEA2 and LEA4 protein family groups. We employed online tools to analyse
physicochemical characteristics (Expasy, ProtParam, BioPython, GRAVY calculator), disorder
propensity, and characterization protein structures (FELLS, JPred, SOPMA, PsiPred, Phyre2,
Espritz-DisProt, Espritz-X, Iupred, TMHMM, +Heliquest).
The most abundant, atypical LEA2 group containing 127, mostly hydrophobic proteins, was
divided into five subgroups. Members of this group were predicted to fold into globular
domains, β-barrel at the C-terminus, followed by transmembrane hydrophobic-helices and
disordered N-terminal regions. Results indicated the possible involvement in the protection
of the chloroplastic membranes.
The LEA4 group exhibited an exceptionally high tendency to form amphipathic α-helices and
simultaneously had a high disorder propensity. This group is made of 96 proteins, classified into 3
subgroups. The high content of polar and charged amino acids (lysine, glutamate, and aspartate) is
characteristic of this group. Motifs corresponding to the R. serbica LEA4 protein family group folded
into A-type α-helices that contained positive, negative, and hydrophobic surfaces. Based on previous
knowledge, the possible functions of the LEA2 and LEA4 groups are discussed with significant
implications on cell preservation technology and the improvement of crop drought tolerance.",
publisher = "Belgrade : Institute of molecular genetics and genetic engineering",
journal = "4th Belgrade Bioinformatics Conference",
title = "Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.",
pages = "68-68",
volume = "4",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2008"
}

Pantelić, A., Stevanović, S., Milić Komić, S., Kilibarda, N.,& Vidović, M.. (2023). Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.. in 4th Belgrade Bioinformatics Conference
Belgrade : Institute of molecular genetics and genetic engineering., 4, 68-68.
https://hdl.handle.net/21.15107/rcub_imagine_2008

Pantelić A, Stevanović S, Milić Komić S, Kilibarda N, Vidović M. Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.. in 4th Belgrade Bioinformatics Conference. 2023;4:68-68.
https://hdl.handle.net/21.15107/rcub_imagine_2008 .

Pantelić, Ana, Stevanović, Strahinja, Milić Komić, Sonja, Kilibarda, Nataša, Vidović, Marija, "Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc." in 4th Belgrade Bioinformatics Conference, 4 (2023):68-68,
https://hdl.handle.net/21.15107/rcub_imagine_2008 .

TY  - CONF
AU  - Pantelić, Ana
AU  - Senćanski, Milan
AU  - Prodić, Ivana
AU  - Milić, Dejana
AU  - Vidović, Marija
PY  - 2023
UR  - https://ml4ngp.eu/conference-bratislava/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1934
PB  - European Cooperation in Science and Technology
C3  - Non-globular proteins in the era of machine learning
T1  - Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation
EP  - 6
SP  - 5
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1934
ER  - 

@conference{
author = "Pantelić, Ana and Senćanski, Milan and Prodić, Ivana and Milić, Dejana and Vidović, Marija",
year = "2023",
publisher = "European Cooperation in Science and Technology",
journal = "Non-globular proteins in the era of machine learning",
title = "Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation",
pages = "6-5",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1934"
}

Pantelić, A., Senćanski, M., Prodić, I., Milić, D.,& Vidović, M.. (2023). Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation. in Non-globular proteins in the era of machine learning
European Cooperation in Science and Technology., 5-6.
https://hdl.handle.net/21.15107/rcub_imagine_1934

Pantelić A, Senćanski M, Prodić I, Milić D, Vidović M. Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation. in Non-globular proteins in the era of machine learning. 2023;:5-6.
https://hdl.handle.net/21.15107/rcub_imagine_1934 .

Pantelić, Ana, Senćanski, Milan, Prodić, Ivana, Milić, Dejana, Vidović, Marija, "Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation" in Non-globular proteins in the era of machine learning (2023):5-6,
https://hdl.handle.net/21.15107/rcub_imagine_1934 .

TY  - CONF
AU  - Vidović, Marija
AU  - Pantelić, Ana
AU  - Senćanski, Milan
AU  - Prodić, Ivana
PY  - 2023
UR  - https://ml4ngp.eu/conference-bratislava/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1933
PB  - European Cooperation in Science and Technology
C3  - Non-globular proteins in the era of machine learning
T1  - LEA4 proteins: How disordered are they?
EP  - 50
SP  - 49
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1933
ER  - 

@conference{
author = "Vidović, Marija and Pantelić, Ana and Senćanski, Milan and Prodić, Ivana",
year = "2023",
publisher = "European Cooperation in Science and Technology",
journal = "Non-globular proteins in the era of machine learning",
title = "LEA4 proteins: How disordered are they?",
pages = "50-49",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1933"
}

Vidović, M., Pantelić, A., Senćanski, M.,& Prodić, I.. (2023). LEA4 proteins: How disordered are they?. in Non-globular proteins in the era of machine learning
European Cooperation in Science and Technology., 49-50.
https://hdl.handle.net/21.15107/rcub_imagine_1933

Vidović M, Pantelić A, Senćanski M, Prodić I. LEA4 proteins: How disordered are they?. in Non-globular proteins in the era of machine learning. 2023;:49-50.
https://hdl.handle.net/21.15107/rcub_imagine_1933 .

Vidović, Marija, Pantelić, Ana, Senćanski, Milan, Prodić, Ivana, "LEA4 proteins: How disordered are they?" in Non-globular proteins in the era of machine learning (2023):49-50,
https://hdl.handle.net/21.15107/rcub_imagine_1933 .

TY  - CONF
AU  - Vidović, Marija
AU  - Tosti, T.
AU  - Nikolić, N.
AU  - Pantelić, Ana
AU  - Veljović Jovanović, S.
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1868
UR  - http://www.sfses.com/docs/14th-SFSES-Abstracts.pdf
AB  - Resurrection plant Ramonda serbica Panc. survives long desiccation periods
and fully recovers metabolic functions already one day upon watering. This study
aimed to investigate the role of soluble sugars and polyphenols, as well as cell wallassociated
polysaccharides and lignin in desiccation tolerance in R. serbica, an
endemic species from the Balkan peninsula. We combined differential
transcriptomics and proteomics, the analysis of soluble polyphenolics and sugars, as
well as FTIR analysis of the cell wall polymers. Pectin, cellulose, hemicellulose, and
xyloglucans were identified as polysaccharide components of the R. serbica cell
wall and they decreased upon desiccation. Desiccation provoked cell wall
remodelling related to the possible production of H2O2/HO via germin-like proteins
and pectin demethylesterification. In addition, desiccation induced carbon recycling
from starch to soluble sugar osmolytes, whose content significantly increased in
desiccated leaves. These data support the importance of specific sugars and the
plasticity of the cell wall as one of the major contributors to desiccation tolerance of
resurrection species, contributing to further crop drought tolerance improvement.
PB  - Belgrade : Institute for Nature Conservation of Serbia
PB  - Niš : Department of Biology and Ecology, Faculty of Sciences and Mathematics, University of Niš
C3  - 14th Symposium on the Flora of Southeastern Serbia and Neighboring Regions
T1  - The role of polyphenols, sugars, and cell-wall associated polymers in desiccation tolerance of Ramonda serbica
SP  - 73
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1868
ER  - 

@conference{
author = "Vidović, Marija and Tosti, T. and Nikolić, N. and Pantelić, Ana and Veljović Jovanović, S.",
year = "2022",
abstract = "Resurrection plant Ramonda serbica Panc. survives long desiccation periods
and fully recovers metabolic functions already one day upon watering. This study
aimed to investigate the role of soluble sugars and polyphenols, as well as cell wallassociated
polysaccharides and lignin in desiccation tolerance in R. serbica, an
endemic species from the Balkan peninsula. We combined differential
transcriptomics and proteomics, the analysis of soluble polyphenolics and sugars, as
well as FTIR analysis of the cell wall polymers. Pectin, cellulose, hemicellulose, and
xyloglucans were identified as polysaccharide components of the R. serbica cell
wall and they decreased upon desiccation. Desiccation provoked cell wall
remodelling related to the possible production of H2O2/HO via germin-like proteins
and pectin demethylesterification. In addition, desiccation induced carbon recycling
from starch to soluble sugar osmolytes, whose content significantly increased in
desiccated leaves. These data support the importance of specific sugars and the
plasticity of the cell wall as one of the major contributors to desiccation tolerance of
resurrection species, contributing to further crop drought tolerance improvement.",
publisher = "Belgrade : Institute for Nature Conservation of Serbia, Niš : Department of Biology and Ecology, Faculty of Sciences and Mathematics, University of Niš",
journal = "14th Symposium on the Flora of Southeastern Serbia and Neighboring Regions",
title = "The role of polyphenols, sugars, and cell-wall associated polymers in desiccation tolerance of Ramonda serbica",
pages = "73",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1868"
}

Vidović, M., Tosti, T., Nikolić, N., Pantelić, A.,& Veljović Jovanović, S.. (2022). The role of polyphenols, sugars, and cell-wall associated polymers in desiccation tolerance of Ramonda serbica. in 14th Symposium on the Flora of Southeastern Serbia and Neighboring Regions
Belgrade : Institute for Nature Conservation of Serbia., 73.
https://hdl.handle.net/21.15107/rcub_imagine_1868

Vidović M, Tosti T, Nikolić N, Pantelić A, Veljović Jovanović S. The role of polyphenols, sugars, and cell-wall associated polymers in desiccation tolerance of Ramonda serbica. in 14th Symposium on the Flora of Southeastern Serbia and Neighboring Regions. 2022;:73.
https://hdl.handle.net/21.15107/rcub_imagine_1868 .

Vidović, Marija, Tosti, T., Nikolić, N., Pantelić, Ana, Veljović Jovanović, S., "The role of polyphenols, sugars, and cell-wall associated polymers in desiccation tolerance of Ramonda serbica" in 14th Symposium on the Flora of Southeastern Serbia and Neighboring Regions (2022):73,
https://hdl.handle.net/21.15107/rcub_imagine_1868 .

TY  - CONF
AU  - Savić, Aleksa
AU  - Vidović, Marija
AU  - Radosavljević, Jelena
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1854
AB  - Fluorescentno obeleženi proteini su neprocenjivi alati u laboratorijskoj praksi za in vivo lokalizovanje i ispitivanje interakcija proteina. Dizajnirali smo vektor za ekspresiju mCerulean3 sa N-terminalnim heksahistidinskim obeleživacem fuzionisanim preko poliasparaginskog linkera i proteolitickog mesta za proteazu virusa graviranosti duvana (TEV) sa -sinukleinom. Ovaj konstrukt može se upotrebiti za proizvodnju -sinukleina nativne sekvence nakon proteolize TEV proteazom. Gen za mCerulean3 je nizom lancanih reakcija polimeraze (SOEing PCR) fuzionisan sa genom za -sinuklein i nakon amplifikacije ukloniran u plazmid pDUET-1. Escherichia coli BL21(DE3) je, nakon transformacije ovim konstruktom, upotrebljena za proizvodnju himernog proteina koji je zadržao fluorescentna svojstva sa prinosom od ~2 mg po litru medijuma nakon precišcavanja imobilizovanom metal-afinitetnom hromatografijom (elektroforetska cistoca: ~80%). Ovaj himerni protein je uspešno proteolizovan TEV proteazom.
AB  - Fluorescently labeled proteins are invaluable tools in laboratory practice to assess the in vivo localization and the interactions of proteins. Here we have designed an expression vector with an N-terminal hexahistidine-tagged mCerulean3 fused through a polyasparagine linker and the proteolytic site of tobacco etch virus protease (TEV) to - synuclein. This construct can be used to produce -synuclein of a native sequence after proteolysis with TEV protease. After fusion of the genes for mCerulean3 and -synuclein through a series of polymerase chain reactions (SOEing PCR), the resulting gene for the chimeric protein was cloned into the pDUET-1 plasmid. Escherichia coli BL21(DE3), upon transformation with this construct, can be used to produce the chimeric protein that retained the fluorescent properties of mCerulean3, with a yield of ~2 mg per liter of medium after purification by immobilized metal-affinity chromatography (electrophoretic purity: ~80%). This chimeric protein was successfully proteolyzed by TEV protease.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine
T1  - Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli
T1  - Cloning and expression of fluorescently labeled )-synuclein in Eschierichia coli
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1854
ER  - 

@conference{
author = "Savić, Aleksa and Vidović, Marija and Radosavljević, Jelena",
year = "2022",
abstract = "Fluorescentno obeleženi proteini su neprocenjivi alati u laboratorijskoj praksi za in vivo lokalizovanje i ispitivanje interakcija proteina. Dizajnirali smo vektor za ekspresiju mCerulean3 sa N-terminalnim heksahistidinskim obeleživacem fuzionisanim preko poliasparaginskog linkera i proteolitickog mesta za proteazu virusa graviranosti duvana (TEV) sa -sinukleinom. Ovaj konstrukt može se upotrebiti za proizvodnju -sinukleina nativne sekvence nakon proteolize TEV proteazom. Gen za mCerulean3 je nizom lancanih reakcija polimeraze (SOEing PCR) fuzionisan sa genom za -sinuklein i nakon amplifikacije ukloniran u plazmid pDUET-1. Escherichia coli BL21(DE3) je, nakon transformacije ovim konstruktom, upotrebljena za proizvodnju himernog proteina koji je zadržao fluorescentna svojstva sa prinosom od ~2 mg po litru medijuma nakon precišcavanja imobilizovanom metal-afinitetnom hromatografijom (elektroforetska cistoca: ~80%). Ovaj himerni protein je uspešno proteolizovan TEV proteazom., Fluorescently labeled proteins are invaluable tools in laboratory practice to assess the in vivo localization and the interactions of proteins. Here we have designed an expression vector with an N-terminal hexahistidine-tagged mCerulean3 fused through a polyasparagine linker and the proteolytic site of tobacco etch virus protease (TEV) to - synuclein. This construct can be used to produce -synuclein of a native sequence after proteolysis with TEV protease. After fusion of the genes for mCerulean3 and -synuclein through a series of polymerase chain reactions (SOEing PCR), the resulting gene for the chimeric protein was cloned into the pDUET-1 plasmid. Escherichia coli BL21(DE3), upon transformation with this construct, can be used to produce the chimeric protein that retained the fluorescent properties of mCerulean3, with a yield of ~2 mg per liter of medium after purification by immobilized metal-affinity chromatography (electrophoretic purity: ~80%). This chimeric protein was successfully proteolyzed by TEV protease.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine",
title = "Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli, Cloning and expression of fluorescently labeled )-synuclein in Eschierichia coli",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1854"
}

Savić, A., Vidović, M.,& Radosavljević, J.. (2022). Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli. in 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine
Beograd : Srpsko hemijsko društvo..
https://hdl.handle.net/21.15107/rcub_imagine_1854

Savić A, Vidović M, Radosavljević J. Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli. in 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine. 2022;.
https://hdl.handle.net/21.15107/rcub_imagine_1854 .

Savić, Aleksa, Vidović, Marija, Radosavljević, Jelena, "Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli" in 58. Savetovanje Srpskog hemijskog društva, Beograd 9. i 10. jun 2022. godine (2022),
https://hdl.handle.net/21.15107/rcub_imagine_1854 .

TY  - CONF
AU  - Milić Komić, Sonja
AU  - Veljović Jovanović, Sonja
AU  - Pantelić, Ana
AU  - Vidović, Marija
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1867
AB  - Ressurection plants are extraordinary because of their ability to withstand long periods
without water, enter a state of anhydrobiosis, and fully recover upon water arrival.
Ramonda serbica is a relic and endemic species that belong to a very small group of
desiccation-tolerant plants in Europe. Underlying physiological, molecular and
morphological mechanisms that enable these plants to survive harsh environmental
conditions have been an appealing subject to many researchers. Most of the genes
responsible for this amazing ability are present in other plants, and this path of research
where those genes could be activated in crops is growing much more attention because of
the imminent crisis regarding food supplies in the near future. Key components involved in
the response to dehydration in R. serbica plants were analysed through a comprehensive
transcriptomic, proteomic, metabolite and photosynthetic study. Late embryogenesis
abundant proteins play a significant role in the complex defence processes involved in
desiccation tolerance. Defining physicochemical characteristics and specific physiological
functions of late embryogenesis abundant proteins – LEAPs may lead to their applicability
in other areas of research.
PB  - Belgrade : Faculty of Chemistry, Serbian Biochemical Societ
C3  - Amazing Biochemistry
T1  - Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein
SP  - 37
VL  - 11
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1867
ER  - 

@conference{
author = "Milić Komić, Sonja and Veljović Jovanović, Sonja and Pantelić, Ana and Vidović, Marija",
year = "2022",
abstract = "Ressurection plants are extraordinary because of their ability to withstand long periods
without water, enter a state of anhydrobiosis, and fully recover upon water arrival.
Ramonda serbica is a relic and endemic species that belong to a very small group of
desiccation-tolerant plants in Europe. Underlying physiological, molecular and
morphological mechanisms that enable these plants to survive harsh environmental
conditions have been an appealing subject to many researchers. Most of the genes
responsible for this amazing ability are present in other plants, and this path of research
where those genes could be activated in crops is growing much more attention because of
the imminent crisis regarding food supplies in the near future. Key components involved in
the response to dehydration in R. serbica plants were analysed through a comprehensive
transcriptomic, proteomic, metabolite and photosynthetic study. Late embryogenesis
abundant proteins play a significant role in the complex defence processes involved in
desiccation tolerance. Defining physicochemical characteristics and specific physiological
functions of late embryogenesis abundant proteins – LEAPs may lead to their applicability
in other areas of research.",
publisher = "Belgrade : Faculty of Chemistry, Serbian Biochemical Societ",
journal = "Amazing Biochemistry",
title = "Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein",
pages = "37",
volume = "11",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1867"
}

Milić Komić, S., Veljović Jovanović, S., Pantelić, A.,& Vidović, M.. (2022). Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein. in Amazing Biochemistry
Belgrade : Faculty of Chemistry, Serbian Biochemical Societ., 11, 37.
https://hdl.handle.net/21.15107/rcub_imagine_1867

Milić Komić S, Veljović Jovanović S, Pantelić A, Vidović M. Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein. in Amazing Biochemistry. 2022;11:37.
https://hdl.handle.net/21.15107/rcub_imagine_1867 .

Milić Komić, Sonja, Veljović Jovanović, Sonja, Pantelić, Ana, Vidović, Marija, "Late embryogenesis abundant proteins: Structural characterisation and interaction with α-synuclein" in Amazing Biochemistry, 11 (2022):37,
https://hdl.handle.net/21.15107/rcub_imagine_1867 .

TY  - CONF
AU  - Savić, Aleksa D.
AU  - Vidović, Marija
AU  - Radosavljević, Jelena
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1832
AB  - Fluorescentno obeleženi proteini su neprocenjivi alati u laboratorijskoj praksi za in vivo lokalizovanje i ispitivanje interakcija proteina. Dizajnirali smo vektor za ekspresiju mCerulean3 sa N-terminalnim heksahistidinskim obeleživacem fuzionisanim preko poliasparaginskog linkera i proteolitickog mesta za proteazu virusa graviranosti duvana (TEV) sa -sinukleinom. Ovaj konstrukt može se upotrebiti za proizvodnju -sinukleina nativne sekvence nakon proteolize TEV proteazom. Gen za mCerulean3 je nizom lancanih reakcija polimeraze (SOEing PCR) fuzionisan sa genom za -sinuklein i nakon amplifikacije ukloniran u plazmid pDUET-1. Escherichia coli BL21(DE3) je, nakon transformacije ovim konstruktom, upotrebljena za proizvodnju himernog proteina koji je zadržao fluorescentna svojstva sa prinosom od ~2 mg po litru medijuma nakon precišcavanja imobilizovanom metal-afinitetnom hromatografijom (elektroforetska cistoca: ~80%). Ovaj himerni protein je uspešno proteolizovan TEV proteazom.
AB  - Fluorescently labeled proteins are invaluable tools in laboratory practice to assess the in vivo localization and the interactions of proteins. Here we have designed an expression vector with an N-terminal hexahistidine-tagged mCerulean3 fused through a polyasparagine linker and the proteolytic site of tobacco etch virus protease (TEV) to - synuclein. This construct can be used to produce -synuclein of a native sequence after proteolysis with TEV protease. After fusion of the genes for mCerulean3 and -synuclein through a series of polymerase chain reactions (SOEing PCR), the resulting gene for the chimeric protein was cloned into the pDUET-1 plasmid. Escherichia coli BL21(DE3), upon transformation with this construct, can be used to produce the chimeric protein that retained the fluorescent properties of mCerulean3, with a yield of ~2 mg per liter of medium after purification by immobilized metal-affinity chromatography (electrophoretic purity: ~80%). This chimeric protein was successfully proteolyzed by TEV protease.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
T1  - Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli
T1  - Cloning and expression of fluorescently labeled )-synuclein in Eschierichia coli
EP  - 68
SP  - 68
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1832
ER  - 

@conference{
author = "Savić, Aleksa D. and Vidović, Marija and Radosavljević, Jelena",
year = "2022",
abstract = "Fluorescentno obeleženi proteini su neprocenjivi alati u laboratorijskoj praksi za in vivo lokalizovanje i ispitivanje interakcija proteina. Dizajnirali smo vektor za ekspresiju mCerulean3 sa N-terminalnim heksahistidinskim obeleživacem fuzionisanim preko poliasparaginskog linkera i proteolitickog mesta za proteazu virusa graviranosti duvana (TEV) sa -sinukleinom. Ovaj konstrukt može se upotrebiti za proizvodnju -sinukleina nativne sekvence nakon proteolize TEV proteazom. Gen za mCerulean3 je nizom lancanih reakcija polimeraze (SOEing PCR) fuzionisan sa genom za -sinuklein i nakon amplifikacije ukloniran u plazmid pDUET-1. Escherichia coli BL21(DE3) je, nakon transformacije ovim konstruktom, upotrebljena za proizvodnju himernog proteina koji je zadržao fluorescentna svojstva sa prinosom od ~2 mg po litru medijuma nakon precišcavanja imobilizovanom metal-afinitetnom hromatografijom (elektroforetska cistoca: ~80%). Ovaj himerni protein je uspešno proteolizovan TEV proteazom., Fluorescently labeled proteins are invaluable tools in laboratory practice to assess the in vivo localization and the interactions of proteins. Here we have designed an expression vector with an N-terminal hexahistidine-tagged mCerulean3 fused through a polyasparagine linker and the proteolytic site of tobacco etch virus protease (TEV) to - synuclein. This construct can be used to produce -synuclein of a native sequence after proteolysis with TEV protease. After fusion of the genes for mCerulean3 and -synuclein through a series of polymerase chain reactions (SOEing PCR), the resulting gene for the chimeric protein was cloned into the pDUET-1 plasmid. Escherichia coli BL21(DE3), upon transformation with this construct, can be used to produce the chimeric protein that retained the fluorescent properties of mCerulean3, with a yield of ~2 mg per liter of medium after purification by immobilized metal-affinity chromatography (electrophoretic purity: ~80%). This chimeric protein was successfully proteolyzed by TEV protease.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine",
title = "Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli, Cloning and expression of fluorescently labeled )-synuclein in Eschierichia coli",
pages = "68-68",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1832"
}

Savić, A. D., Vidović, M.,& Radosavljević, J.. (2022). Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
Beograd : Srpsko hemijsko društvo., 68-68.
https://hdl.handle.net/21.15107/rcub_imagine_1832

Savić AD, Vidović M, Radosavljević J. Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine. 2022;:68-68.
https://hdl.handle.net/21.15107/rcub_imagine_1832 .

Savić, Aleksa D., Vidović, Marija, Radosavljević, Jelena, "Kloniranje i ekspresija fluorescentno obeleženog )-sinukleina u bakteriji Escherichia coli" in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine (2022):68-68,
https://hdl.handle.net/21.15107/rcub_imagine_1832 .

TY  - CONF
AU  - Savić, Aleksa
AU  - Vidović, Marija
AU  - Radosavljević, Jelena
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1831
AB  - Alpha-synuclein is an intrinsically disordered protein prone to aggregation and it is involved in the formation of brain tissue amyloids in patients with Parkinson's and other neurodegenerative diseases. By fluorescently labeling recombinantly expressed proteins, the processes of expression and purification of the same can be easily visually monitored. In a previous work, we have constructed three plasmids for the expression of α-synuclein fused C-terminally to His-tagged mCerulean3 through a polyasparagine linker and tobacco etch virus (TEV) proteolytic site. Here we have transformed these vectors into Escherichia coli BL21(DE3) and BL21(DE3)pLysS and optimized the expression conditions by response surface methodology (temperature, time after induction, concentration of induction reagent) of the chimeric proteins coded by vectors. Expression of the chimeric protein was tested at optimal conditions in different media and terrific broth gave the highest yield. The obtained chimeric protein was purified by immobilized metal-affinity chromatography (IMAC), yielding ~29 mg of chimeric protein per liter of medium and was shown to be successfully proteolyzed by TEV protease, giving a fragment of α-synuclein of expected electrophoretic mobility. After another round of IMAC, the obtained α-synuclein of native sequence was mainly found to be in the flow-through.
PB  - Serbian Chemical Society
PB  - Serbian Young Chemists’ Club
C3  - 8th Conference of Young Chemists of Serbia, 29th October 2022, Belgrade
T1  - Optimization of the expression conditions of fluorescently labeled α-synuclein in Escherichia coli by response surface methodology and proteolysis by tobacco etch virus protease
EP  - 10
SP  - 10
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1831
ER  - 

@conference{
author = "Savić, Aleksa and Vidović, Marija and Radosavljević, Jelena",
year = "2022",
abstract = "Alpha-synuclein is an intrinsically disordered protein prone to aggregation and it is involved in the formation of brain tissue amyloids in patients with Parkinson's and other neurodegenerative diseases. By fluorescently labeling recombinantly expressed proteins, the processes of expression and purification of the same can be easily visually monitored. In a previous work, we have constructed three plasmids for the expression of α-synuclein fused C-terminally to His-tagged mCerulean3 through a polyasparagine linker and tobacco etch virus (TEV) proteolytic site. Here we have transformed these vectors into Escherichia coli BL21(DE3) and BL21(DE3)pLysS and optimized the expression conditions by response surface methodology (temperature, time after induction, concentration of induction reagent) of the chimeric proteins coded by vectors. Expression of the chimeric protein was tested at optimal conditions in different media and terrific broth gave the highest yield. The obtained chimeric protein was purified by immobilized metal-affinity chromatography (IMAC), yielding ~29 mg of chimeric protein per liter of medium and was shown to be successfully proteolyzed by TEV protease, giving a fragment of α-synuclein of expected electrophoretic mobility. After another round of IMAC, the obtained α-synuclein of native sequence was mainly found to be in the flow-through.",
publisher = "Serbian Chemical Society, Serbian Young Chemists’ Club",
journal = "8th Conference of Young Chemists of Serbia, 29th October 2022, Belgrade",
title = "Optimization of the expression conditions of fluorescently labeled α-synuclein in Escherichia coli by response surface methodology and proteolysis by tobacco etch virus protease",
pages = "10-10",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1831"
}

Savić, A., Vidović, M.,& Radosavljević, J.. (2022). Optimization of the expression conditions of fluorescently labeled α-synuclein in Escherichia coli by response surface methodology and proteolysis by tobacco etch virus protease. in 8th Conference of Young Chemists of Serbia, 29th October 2022, Belgrade
Serbian Chemical Society., 10-10.
https://hdl.handle.net/21.15107/rcub_imagine_1831

Savić A, Vidović M, Radosavljević J. Optimization of the expression conditions of fluorescently labeled α-synuclein in Escherichia coli by response surface methodology and proteolysis by tobacco etch virus protease. in 8th Conference of Young Chemists of Serbia, 29th October 2022, Belgrade. 2022;:10-10.
https://hdl.handle.net/21.15107/rcub_imagine_1831 .

Savić, Aleksa, Vidović, Marija, Radosavljević, Jelena, "Optimization of the expression conditions of fluorescently labeled α-synuclein in Escherichia coli by response surface methodology and proteolysis by tobacco etch virus protease" in 8th Conference of Young Chemists of Serbia, 29th October 2022, Belgrade (2022):10-10,
https://hdl.handle.net/21.15107/rcub_imagine_1831 .

TY  - JOUR
AU  - Vidović, Marija
AU  - Battisti, Ilaria
AU  - Pantelić, Ana
AU  - Morina, Filis
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović-Jovanović, Sonja
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1604
AB  - The resurrection plant Ramonda serbica Panc. survives long desiccation periods and fully recovers metabolic functions within one day upon watering. This study aimed to identify key candidates and pathways involved in desiccation tolerance in R. serbica. We combined differential transcriptomics and proteomics, phenolic and sugar analysis, FTIR analysis of the cell wall polymers, and detailed analysis of the photosynthetic electron transport (PET) chain. The proteomic analysis allowed the relative quantification of 1192 different protein groups, of which 408 were differentially abundant between hydrated (HL) and desiccated leaves (DL). Almost all differentially abundant proteins related to photosynthetic processes were less abundant, while chlorophyll fluorescence measurements implied shifting from linear PET to cyclic electron transport (CET). The levels of H2O2 scavenging enzymes, ascorbate-glutathione cycle components, catalases, peroxiredoxins, Fe-, and Mn superoxide dismutase (SOD) were reduced in DL. However, six germin-like proteins (GLPs), four Cu/ ZnSOD isoforms, three polyphenol oxidases, and 22 late embryogenesis abundant proteins (LEAPs; mainly LEA4 and dehydrins), were desiccation-inducible. Desiccation provoked cell wall remodeling related to GLP-derived H2O2/HO center dot activity and pectin demethylesterification. This comprehensive study contributes to understanding the role and regulation of the main metabolic pathways during desiccation aiming at crop drought tolerance improvement.
PB  - MDPI, Basel
T2  - Plants-Basel
T1  - Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study
IS  - 9
VL  - 11
DO  - 10.3390/plants11091199
ER  - 

@article{
author = "Vidović, Marija and Battisti, Ilaria and Pantelić, Ana and Morina, Filis and Arrigoni, Giorgio and Masi, Antonio and Veljović-Jovanović, Sonja",
year = "2022",
abstract = "The resurrection plant Ramonda serbica Panc. survives long desiccation periods and fully recovers metabolic functions within one day upon watering. This study aimed to identify key candidates and pathways involved in desiccation tolerance in R. serbica. We combined differential transcriptomics and proteomics, phenolic and sugar analysis, FTIR analysis of the cell wall polymers, and detailed analysis of the photosynthetic electron transport (PET) chain. The proteomic analysis allowed the relative quantification of 1192 different protein groups, of which 408 were differentially abundant between hydrated (HL) and desiccated leaves (DL). Almost all differentially abundant proteins related to photosynthetic processes were less abundant, while chlorophyll fluorescence measurements implied shifting from linear PET to cyclic electron transport (CET). The levels of H2O2 scavenging enzymes, ascorbate-glutathione cycle components, catalases, peroxiredoxins, Fe-, and Mn superoxide dismutase (SOD) were reduced in DL. However, six germin-like proteins (GLPs), four Cu/ ZnSOD isoforms, three polyphenol oxidases, and 22 late embryogenesis abundant proteins (LEAPs; mainly LEA4 and dehydrins), were desiccation-inducible. Desiccation provoked cell wall remodeling related to GLP-derived H2O2/HO center dot activity and pectin demethylesterification. This comprehensive study contributes to understanding the role and regulation of the main metabolic pathways during desiccation aiming at crop drought tolerance improvement.",
publisher = "MDPI, Basel",
journal = "Plants-Basel",
title = "Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study",
number = "9",
volume = "11",
doi = "10.3390/plants11091199"
}

Vidović, M., Battisti, I., Pantelić, A., Morina, F., Arrigoni, G., Masi, A.,& Veljović-Jovanović, S.. (2022). Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study. in Plants-Basel
MDPI, Basel., 11(9).
https://doi.org/10.3390/plants11091199

Vidović M, Battisti I, Pantelić A, Morina F, Arrigoni G, Masi A, Veljović-Jovanović S. Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study. in Plants-Basel. 2022;11(9).
doi:10.3390/plants11091199 .

Vidović, Marija, Battisti, Ilaria, Pantelić, Ana, Morina, Filis, Arrigoni, Giorgio, Masi, Antonio, Veljović-Jovanović, Sonja, "Desiccation Tolerance in Ramonda serbica Panc.: An Integrative Transcriptomic, Proteomic, Metabolite and Photosynthetic Study" in Plants-Basel, 11, no. 9 (2022),
https://doi.org/10.3390/plants11091199 . .

TY  - JOUR
AU  - Vidović, Marija
AU  - Rikalović, Milena G.
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1598
AB  - Following Alzheimer's, Parkinson's disease (PD) is the second-most common neurodegenerative disorder, sharing an unclear pathophysiology, a multifactorial profile, and massive social costs worldwide. Despite this, no disease-modifying therapy is available. PD is tightly associated with alpha-synuclein (alpha-Syn) deposits, which become organised into insoluble, amyloid fibrils. As a typical intrinsically disordered protein, alpha-Syn adopts a monomeric, random coil conformation in an aqueous solution, while its interaction with lipid membranes drives the transition of the molecule part into an alpha-helical structure. The central unstructured region of alpha-Syn is involved in fibril formation by converting to well-defined, beta-sheet rich secondary structures. Presently, most therapeutic strategies against PD are focused on designing small molecules, peptides, and peptidomimetics that can directly target alpha-Syn and its aggregation pathway. Other approaches include gene silencing, cell transplantation, stimulation of intracellular clearance with autophagy promoters, and degradation pathways based on immunotherapy of amyloid fibrils. In the present review, we summarise the current advances related to alpha-Syn aggregation/neurotoxicity. These findings present a valuable arsenal for the further development of efficient, nontoxic, and non-invasive therapeutic protocols for disease-modifying therapy that tackles disease onset and progression in the future.
PB  - MDPI, Basel
T2  - Cells
T1  - Alpha-Synuclein Aggregation Pathway in Parkinson's Disease: Current Status and Novel Therapeutic Approaches
IS  - 11
VL  - 11
DO  - 10.3390/cells11111732
ER  - 

@article{
author = "Vidović, Marija and Rikalović, Milena G.",
year = "2022",
abstract = "Following Alzheimer's, Parkinson's disease (PD) is the second-most common neurodegenerative disorder, sharing an unclear pathophysiology, a multifactorial profile, and massive social costs worldwide. Despite this, no disease-modifying therapy is available. PD is tightly associated with alpha-synuclein (alpha-Syn) deposits, which become organised into insoluble, amyloid fibrils. As a typical intrinsically disordered protein, alpha-Syn adopts a monomeric, random coil conformation in an aqueous solution, while its interaction with lipid membranes drives the transition of the molecule part into an alpha-helical structure. The central unstructured region of alpha-Syn is involved in fibril formation by converting to well-defined, beta-sheet rich secondary structures. Presently, most therapeutic strategies against PD are focused on designing small molecules, peptides, and peptidomimetics that can directly target alpha-Syn and its aggregation pathway. Other approaches include gene silencing, cell transplantation, stimulation of intracellular clearance with autophagy promoters, and degradation pathways based on immunotherapy of amyloid fibrils. In the present review, we summarise the current advances related to alpha-Syn aggregation/neurotoxicity. These findings present a valuable arsenal for the further development of efficient, nontoxic, and non-invasive therapeutic protocols for disease-modifying therapy that tackles disease onset and progression in the future.",
publisher = "MDPI, Basel",
journal = "Cells",
title = "Alpha-Synuclein Aggregation Pathway in Parkinson's Disease: Current Status and Novel Therapeutic Approaches",
number = "11",
volume = "11",
doi = "10.3390/cells11111732"
}

Vidović, M.,& Rikalović, M. G.. (2022). Alpha-Synuclein Aggregation Pathway in Parkinson's Disease: Current Status and Novel Therapeutic Approaches. in Cells
MDPI, Basel., 11(11).
https://doi.org/10.3390/cells11111732

Vidović M, Rikalović MG. Alpha-Synuclein Aggregation Pathway in Parkinson's Disease: Current Status and Novel Therapeutic Approaches. in Cells. 2022;11(11).
doi:10.3390/cells11111732 .

Vidović, Marija, Rikalović, Milena G., "Alpha-Synuclein Aggregation Pathway in Parkinson's Disease: Current Status and Novel Therapeutic Approaches" in Cells, 11, no. 11 (2022),
https://doi.org/10.3390/cells11111732 . .

TY  - JOUR
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
AU  - Komić, Sonja Milic
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1560
AB  - Ramonda serbica Panc. is an ancient resurrection plant able to survive a long desiccation period and recover metabolic functions upon watering. The accumulation of protective late embryogenesis abundant proteins (LEAPs) is a desiccation tolerance hallmark. To propose their role in R. serbica desiccation tolerance, we structurally characterised LEAPs and evaluated LEA gene expression levels in hydrated and desiccated leaves. By integrating de novo transcriptomics and homologues LEAP domains, 318 R. serbica LEAPs were identified and classified according to their conserved motifs and phylogeny. The in silico analysis revealed that hydrophilic LEA4 proteins exhibited an exceptionally high tendency to form amphipathic alpha-helices. The most abundant, atypical LEA2 group contained more hydrophobic proteins predicted to fold into the defined globular domains. Within the desiccation-upregulated LEA genes, the majority encoded highly disordered DEH1, LEA1, LEA4.2, and LEA4.3 proteins, while the greatest portion of downregulated genes encoded LEA2.3 and LEA2.5 proteins. While dehydrins might chelate metals and bind DNA under water deficit, other intrinsically disordered LEAPs might participate in forming intracellular proteinaceous condensates or adopt amphipathic alpha-helical conformation, enabling them to stabilise desiccation-sensitive proteins and membranes. This comprehensive LEAPs structural characterisation is essential to understanding their function and regulation during desiccation aiming at crop drought tolerance improvement.
PB  - MDPI, Basel
T2  - International Journal of Molecular Sciences
T1  - In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance in Ramonda serbica Panc
IS  - 7
VL  - 23
DO  - 10.3390/ijms23073547
ER  - 

@article{
author = "Pantelić, Ana and Stevanović, Strahinja and Komić, Sonja Milic and Kilibarda, Nataša and Vidović, Marija",
year = "2022",
abstract = "Ramonda serbica Panc. is an ancient resurrection plant able to survive a long desiccation period and recover metabolic functions upon watering. The accumulation of protective late embryogenesis abundant proteins (LEAPs) is a desiccation tolerance hallmark. To propose their role in R. serbica desiccation tolerance, we structurally characterised LEAPs and evaluated LEA gene expression levels in hydrated and desiccated leaves. By integrating de novo transcriptomics and homologues LEAP domains, 318 R. serbica LEAPs were identified and classified according to their conserved motifs and phylogeny. The in silico analysis revealed that hydrophilic LEA4 proteins exhibited an exceptionally high tendency to form amphipathic alpha-helices. The most abundant, atypical LEA2 group contained more hydrophobic proteins predicted to fold into the defined globular domains. Within the desiccation-upregulated LEA genes, the majority encoded highly disordered DEH1, LEA1, LEA4.2, and LEA4.3 proteins, while the greatest portion of downregulated genes encoded LEA2.3 and LEA2.5 proteins. While dehydrins might chelate metals and bind DNA under water deficit, other intrinsically disordered LEAPs might participate in forming intracellular proteinaceous condensates or adopt amphipathic alpha-helical conformation, enabling them to stabilise desiccation-sensitive proteins and membranes. This comprehensive LEAPs structural characterisation is essential to understanding their function and regulation during desiccation aiming at crop drought tolerance improvement.",
publisher = "MDPI, Basel",
journal = "International Journal of Molecular Sciences",
title = "In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance in Ramonda serbica Panc",
number = "7",
volume = "23",
doi = "10.3390/ijms23073547"
}

Pantelić, A., Stevanović, S., Komić, S. M., Kilibarda, N.,& Vidović, M.. (2022). In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance in Ramonda serbica Panc. in International Journal of Molecular Sciences
MDPI, Basel., 23(7).
https://doi.org/10.3390/ijms23073547

Pantelić A, Stevanović S, Komić SM, Kilibarda N, Vidović M. In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance in Ramonda serbica Panc. in International Journal of Molecular Sciences. 2022;23(7).
doi:10.3390/ijms23073547 .

Pantelić, Ana, Stevanović, Strahinja, Komić, Sonja Milic, Kilibarda, Nataša, Vidović, Marija, "In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance in Ramonda serbica Panc" in International Journal of Molecular Sciences, 23, no. 7 (2022),
https://doi.org/10.3390/ijms23073547 . .

TY  - DATA
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
AU  - Milić-Komić, Sonja
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1853
AB  - Ramonda serbica de novo transcriptome database
PB  - MDPI
T2  - International Journal of Molecular Science
T1  - Ramonda serbica de novo transcriptome database related to the article: Pantelic, A.; Stevanović, S.; Milic-Komic, S.; Kilibarda, N.; Vidovic, M. Characterization and expression analysis of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves
VL  - n/a
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1853
ER  - 

@misc{
author = "Pantelić, Ana and Stevanović, Strahinja and Milić-Komić, Sonja and Kilibarda, Nataša and Vidović, Marija",
year = "2022",
abstract = "Ramonda serbica de novo transcriptome database",
publisher = "MDPI",
journal = "International Journal of Molecular Science",
title = "Ramonda serbica de novo transcriptome database related to the article: Pantelic, A.; Stevanović, S.; Milic-Komic, S.; Kilibarda, N.; Vidovic, M. Characterization and expression analysis of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves",
volume = "n/a",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1853"
}

Pantelić, A., Stevanović, S., Milić-Komić, S., Kilibarda, N.,& Vidović, M.. (2022). Ramonda serbica de novo transcriptome database related to the article: Pantelic, A.; Stevanović, S.; Milic-Komic, S.; Kilibarda, N.; Vidovic, M. Characterization and expression analysis of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves. in International Journal of Molecular Science
MDPI., n/a.
https://hdl.handle.net/21.15107/rcub_imagine_1853

Pantelić A, Stevanović S, Milić-Komić S, Kilibarda N, Vidović M. Ramonda serbica de novo transcriptome database related to the article: Pantelic, A.; Stevanović, S.; Milic-Komic, S.; Kilibarda, N.; Vidovic, M. Characterization and expression analysis of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves. in International Journal of Molecular Science. 2022;n/a.
https://hdl.handle.net/21.15107/rcub_imagine_1853 .

Pantelić, Ana, Stevanović, Strahinja, Milić-Komić, Sonja, Kilibarda, Nataša, Vidović, Marija, "Ramonda serbica de novo transcriptome database related to the article: Pantelic, A.; Stevanović, S.; Milic-Komic, S.; Kilibarda, N.; Vidovic, M. Characterization and expression analysis of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves" in International Journal of Molecular Science, n/a (2022),
https://hdl.handle.net/21.15107/rcub_imagine_1853 .

TY  - CONF
AU  - Vidović, Marija
AU  - Battisti, Ilaria
AU  - Pantelić, Ana
AU  - Morina, Filis
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović Jovanović, Sonja
PY  - 2022
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1833
AB  - Ramonda serbica Panc. is a resurrection plant species that can survive desiccation for a longperiod and fully resume metabolic functions upon rewatering in a very short period, even within48 h. The goal of this study was to identify key candidates and pathways involved in desiccation tolerance in R. serbica. To achieve this, systems biology approach combining transcriptomics,proteomics, and analysis of specific metabolites was employed. In addition, FTIR analysis of thecell wall polymers and a detailed analysis of the photosynthetic electron transport (PET) chainwere performed. In total, 1192 different protein groups were quantified by TMT-based comparative quantitative proteomics. Among them, 408 protein groups showed a statistically significantdifference in abundance between hydrated (HL) and desiccated leaves (DL). Upon desiccation, themajority of proteins related to photosynthetic processes were less abundant, while chlorophyllfluorescence measurements implied shifting from linear photosynthetic transport (PET) to cyclicelectron transport (CET). The amounts of H2O2 scavenging enzymes, including ascorbate-glutathione cycle components, catalases, peroxiredoxins, Fe-, and Mn- superoxide dismutase (SOD) werereduced in DL. However, four Cu/ZnSOD isoforms, three polyphenol oxidases, six germin-like proteins (GLPs), and 22 late embryogenesis abundant proteins (LEAPs; mainly LEA4 and dehydrins),were desiccation-inducible. Desiccation-induced cell wall remodelling by changes in cell wallpolymer composition might be linked with pectin demethylesterification and GLP-derived H2O2/HO•. Our study demonstrated that desiccation tolerance in R. serbica is a complex, species-specific process orchestrated by several metabolic pathways and regulatory networks acting at the transcript, protein, metabolite and physiological levels.
C3  - 4th International Conference on Plant Biology and 23rd SPPS Meeting
T1  - Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects
EP  - 27
SP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1833
ER  - 

@conference{
author = "Vidović, Marija and Battisti, Ilaria and Pantelić, Ana and Morina, Filis and Arrigoni, Giorgio and Masi, Antonio and Veljović Jovanović, Sonja",
year = "2022",
abstract = "Ramonda serbica Panc. is a resurrection plant species that can survive desiccation for a longperiod and fully resume metabolic functions upon rewatering in a very short period, even within48 h. The goal of this study was to identify key candidates and pathways involved in desiccation tolerance in R. serbica. To achieve this, systems biology approach combining transcriptomics,proteomics, and analysis of specific metabolites was employed. In addition, FTIR analysis of thecell wall polymers and a detailed analysis of the photosynthetic electron transport (PET) chainwere performed. In total, 1192 different protein groups were quantified by TMT-based comparative quantitative proteomics. Among them, 408 protein groups showed a statistically significantdifference in abundance between hydrated (HL) and desiccated leaves (DL). Upon desiccation, themajority of proteins related to photosynthetic processes were less abundant, while chlorophyllfluorescence measurements implied shifting from linear photosynthetic transport (PET) to cyclicelectron transport (CET). The amounts of H2O2 scavenging enzymes, including ascorbate-glutathione cycle components, catalases, peroxiredoxins, Fe-, and Mn- superoxide dismutase (SOD) werereduced in DL. However, four Cu/ZnSOD isoforms, three polyphenol oxidases, six germin-like proteins (GLPs), and 22 late embryogenesis abundant proteins (LEAPs; mainly LEA4 and dehydrins),were desiccation-inducible. Desiccation-induced cell wall remodelling by changes in cell wallpolymer composition might be linked with pectin demethylesterification and GLP-derived H2O2/HO•. Our study demonstrated that desiccation tolerance in R. serbica is a complex, species-specific process orchestrated by several metabolic pathways and regulatory networks acting at the transcript, protein, metabolite and physiological levels.",
journal = "4th International Conference on Plant Biology and 23rd SPPS Meeting",
title = "Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1833"
}

Vidović, M., Battisti, I., Pantelić, A., Morina, F., Arrigoni, G., Masi, A.,& Veljović Jovanović, S.. (2022). Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects. in 4th International Conference on Plant Biology and 23rd SPPS Meeting, 27-27.
https://hdl.handle.net/21.15107/rcub_imagine_1833

Vidović M, Battisti I, Pantelić A, Morina F, Arrigoni G, Masi A, Veljović Jovanović S. Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects. in 4th International Conference on Plant Biology and 23rd SPPS Meeting. 2022;:27-27.
https://hdl.handle.net/21.15107/rcub_imagine_1833 .

Vidović, Marija, Battisti, Ilaria, Pantelić, Ana, Morina, Filis, Arrigoni, Giorgio, Masi, Antonio, Veljović Jovanović, Sonja, "Mechanisms of desiccation tolerance in Ramonda serbica Panc.: transcriptomic, proteomic, metabolomic, and photosynthetic aspects" in 4th International Conference on Plant Biology and 23rd SPPS Meeting (2022):27-27,
https://hdl.handle.net/21.15107/rcub_imagine_1833 .

TY  - CONF
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2021
UR  - http://ojs.pmf.uns.ac.rs/index.php/dbe_serbica/index
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1856
AB  - An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation, aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding, ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation.Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica by integrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs were classification into six groups according to Protein family (PFAM) database and the most populated group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence length is predicted to form α-helical structure). This implies that charged residues might be exposed to the solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in the cell. In addition, as predicted by several bioinformatic tools, more than 70% of identified LEAPs were found to be highly disordered (~64%). Structural characterization of LEAPs is a key to understand their function and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings will promote transformative advancements in various fields, such as the development of new strategies in neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.
PB  - Novi Sad : Faculty of Sciences, Department of Biology and Ecology
C3  - Biologia Serbica
T1  - De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins
EP  - 65
IS  - 1 (spec. ed.)
SP  - 65
VL  - 43
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1856
ER  - 

@conference{
author = "Pantelić, Ana and Stevanović, Strahinja and Kilibarda, Nataša and Vidović, Marija",
year = "2021",
abstract = "An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation, aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding, ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells during desiccation.Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica by integrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs were classification into six groups according to Protein family (PFAM) database and the most populated group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence length is predicted to form α-helical structure). This implies that charged residues might be exposed to the solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in the cell. In addition, as predicted by several bioinformatic tools, more than 70% of identified LEAPs were found to be highly disordered (~64%). Structural characterization of LEAPs is a key to understand their function and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings will promote transformative advancements in various fields, such as the development of new strategies in neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.",
publisher = "Novi Sad : Faculty of Sciences, Department of Biology and Ecology",
journal = "Biologia Serbica",
title = "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins",
pages = "65-65",
number = "1 (spec. ed.)",
volume = "43",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1856"
}

Pantelić, A., Stevanović, S., Kilibarda, N.,& Vidović, M.. (2021). De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins. in Biologia Serbica
Novi Sad : Faculty of Sciences, Department of Biology and Ecology., 43(1 (spec. ed.)), 65-65.
https://hdl.handle.net/21.15107/rcub_imagine_1856

Pantelić A, Stevanović S, Kilibarda N, Vidović M. De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins. in Biologia Serbica. 2021;43(1 (spec. ed.)):65-65.
https://hdl.handle.net/21.15107/rcub_imagine_1856 .

Pantelić, Ana, Stevanović, Strahinja, Kilibarda, Nataša, Vidović, Marija, "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of Late Embryogenesis Abundant Proteins" in Biologia Serbica, 43, no. 1 (spec. ed.) (2021):65-65,
https://hdl.handle.net/21.15107/rcub_imagine_1856 .

TY  - CHAP
AU  - Vidović, Marija
AU  - Komić Milić, Sonja
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1776
UR  - https://novapublishers.com/shop/a-closer-look-at-proteolysis/
AB  - Proteolysis represents a primary recycling system for amino acids.
Moreover, by controlling the protein turnover, proteolysis plays an
important role in key cellular processes such as control of cell cycle,
programmed cell death (including senescence) and response to various
stimuli. In eukaryotic cells, most proteins are degraded by autophagy and
26S proteasome machinery, composed in general of 20S proteolytic core and 19S regulatory particle. The protein susceptibility to proteolysis is
determined by its structural features. Folded globular proteins in their
native state are rarely degraded, however when misfolded, denatured or
when an unstructured region is attached, the degradation is promoted.
Proteins natively containing intrinsically disordered regions (IDRs) or
completely lacking the stable secondary and tertiary structures are
defined as intrinsically disordered proteins (IDPs). Due to their high
intramolecular flexibility and plasticity, IDPs are involved in DNA
metabolism, transcriptional activation, autophagy, and signalling
cascades related to response to various stimuli. In sessile organisms such
as plants, IDPs enable prompt acclimation to external factors, including
light perception, adaptation to oxidative stress and water loss, and
regulation of protective, antioxidative and secondary metabolism.
Binding of specific ligands and partners to particular IDP triggers
structural changes and affects the stability of IDP, its susceptibility to
proteolysis and aggregation-propensity. Theabnormal aggregation of
several IDPs and altered proteolysis pathways are closely connected with
serious neurodegenerative disorders, such as Alzheimer’s and Parkinson's
diseases. In this chapter, we discuss the current understanding of
proteolytic processes of specific, well-characterised IDPs under different
physiological states, emphasizing the influence of the microenvironment
and ligands/partners on their conformation.
PB  - Nova Science Publishers, Inc.
T2  - A closer look at proteolysis
T1  - Regulation of proteolysis of intrinsically disordered proteins: physiological consequences
EP  - 46
SP  - 1
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1776
ER  - 

@inbook{
author = "Vidović, Marija and Komić Milić, Sonja",
year = "2021",
abstract = "Proteolysis represents a primary recycling system for amino acids.
Moreover, by controlling the protein turnover, proteolysis plays an
important role in key cellular processes such as control of cell cycle,
programmed cell death (including senescence) and response to various
stimuli. In eukaryotic cells, most proteins are degraded by autophagy and
26S proteasome machinery, composed in general of 20S proteolytic core and 19S regulatory particle. The protein susceptibility to proteolysis is
determined by its structural features. Folded globular proteins in their
native state are rarely degraded, however when misfolded, denatured or
when an unstructured region is attached, the degradation is promoted.
Proteins natively containing intrinsically disordered regions (IDRs) or
completely lacking the stable secondary and tertiary structures are
defined as intrinsically disordered proteins (IDPs). Due to their high
intramolecular flexibility and plasticity, IDPs are involved in DNA
metabolism, transcriptional activation, autophagy, and signalling
cascades related to response to various stimuli. In sessile organisms such
as plants, IDPs enable prompt acclimation to external factors, including
light perception, adaptation to oxidative stress and water loss, and
regulation of protective, antioxidative and secondary metabolism.
Binding of specific ligands and partners to particular IDP triggers
structural changes and affects the stability of IDP, its susceptibility to
proteolysis and aggregation-propensity. Theabnormal aggregation of
several IDPs and altered proteolysis pathways are closely connected with
serious neurodegenerative disorders, such as Alzheimer’s and Parkinson's
diseases. In this chapter, we discuss the current understanding of
proteolytic processes of specific, well-characterised IDPs under different
physiological states, emphasizing the influence of the microenvironment
and ligands/partners on their conformation.",
publisher = "Nova Science Publishers, Inc.",
journal = "A closer look at proteolysis",
booktitle = "Regulation of proteolysis of intrinsically disordered proteins: physiological consequences",
pages = "46-1",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1776"
}

Vidović, M.,& Komić Milić, S.. (2021). Regulation of proteolysis of intrinsically disordered proteins: physiological consequences. in A closer look at proteolysis
Nova Science Publishers, Inc.., 1-46.
https://hdl.handle.net/21.15107/rcub_imagine_1776

Vidović M, Komić Milić S. Regulation of proteolysis of intrinsically disordered proteins: physiological consequences. in A closer look at proteolysis. 2021;:1-46.
https://hdl.handle.net/21.15107/rcub_imagine_1776 .

Vidović, Marija, Komić Milić, Sonja, "Regulation of proteolysis of intrinsically disordered proteins: physiological consequences" in A closer look at proteolysis (2021):1-46,
https://hdl.handle.net/21.15107/rcub_imagine_1776 .

TY  - CONF
AU  - Vidović, Marija
AU  - Stevanović, Strahinja
AU  - Pantelić, Ana
AU  - Veljović-Jovanović, Sonja
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1855
AB  - Ramonda serbica Panc. is a resurrection plant that can survive a long period of severe dehydrationdesiccation.Desiccation induces cellular membrane integrity loss, protein aggregation, and denaturation, as well asaccelerated generation of reactive oxygen species. However, R. serbica can fully recover its metabolic functionsalready one day upon watering [1].Aim: to obtain more insight into the mechanisms of desiccation tolerance in R. serbica by differential de novotranscriptomics of hydrated (HL) and desiccated leaves (DL).
C3  - Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia
T1  - De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1855
ER  - 

@conference{
author = "Vidović, Marija and Stevanović, Strahinja and Pantelić, Ana and Veljović-Jovanović, Sonja",
year = "2021",
abstract = "Ramonda serbica Panc. is a resurrection plant that can survive a long period of severe dehydrationdesiccation.Desiccation induces cellular membrane integrity loss, protein aggregation, and denaturation, as well asaccelerated generation of reactive oxygen species. However, R. serbica can fully recover its metabolic functionsalready one day upon watering [1].Aim: to obtain more insight into the mechanisms of desiccation tolerance in R. serbica by differential de novotranscriptomics of hydrated (HL) and desiccated leaves (DL).",
journal = "Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia",
title = "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1855"
}

Vidović, M., Stevanović, S., Pantelić, A.,& Veljović-Jovanović, S.. (2021). De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance. in Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia.
https://hdl.handle.net/21.15107/rcub_imagine_1855

Vidović M, Stevanović S, Pantelić A, Veljović-Jovanović S. De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance. in Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia. 2021;.
https://hdl.handle.net/21.15107/rcub_imagine_1855 .

Vidović, Marija, Stevanović, Strahinja, Pantelić, Ana, Veljović-Jovanović, Sonja, "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance" in Belgrade BioInformatics Conference 2021, 21-25 June, Vinča, Serbia (2021),
https://hdl.handle.net/21.15107/rcub_imagine_1855 .

TY  - CONF
AU  - Stevanović, Strahinja
AU  - Vidović, Marija
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1836
AB  - Desiccation or extreme water loss leads to protein denaturation, aggregation, and degradation and impairs membrane lipid fluidity, resulting in loss of membrane integrity at the cellular level. The induction of late embryogenesis abundant proteins (LEAPs) is considered an essential component of desiccation tolerance strategy in so-called resurrection plants. This heterogeneous group of hydrophilic, non-globular proteins is characterized by a high structural plasticity that allows them to adopt a random conformation in aqueous solutions that transforms into α-helices during dehydration [1]. Therefore, LEAPs can interact with various ligands and partners, including ion sequestration and stabilization of membranes and enzymes during freezing or drying [2]. Our new transcriptome database of an endemic resurrection species Ramonda serbica allowed us to identify 153 members of the LEA gene family. LEAPs of this sample data have an average primary sequence similarity and identity of 10% and 6%, respectively, but with a high variance (141 and 108), which means that the sample proteins can be classified based on domain homology. The averaging is based on multiple sequence alignment and the variance is estimated using pairwise sequence alignment scores. Accordingly, all identified LEAPs were clustered into six groups based on protein families (PFAM). Among these groups, LEAPs differ significantly in their secondary structure, disorder propensity and aggregation potential. Furthermore, we built homology models using Protein Data Bank structure information as templates. For each group, an ensemble of superimposed 3D homology models was analyzed. The information obtained from the representative structural models is key to understanding the function of LEAPs and the regulation of their intrinsic structural disorder-to-order transition during desiccation. This will pave the way for the identification of LEAPs endogenous partners and their targets in the cell and provide further insights into the protective mechanisms of desiccation tolerance.
C3  - Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5
T1  - In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1836
ER  - 

@conference{
author = "Stevanović, Strahinja and Vidović, Marija",
year = "2021",
abstract = "Desiccation or extreme water loss leads to protein denaturation, aggregation, and degradation and impairs membrane lipid fluidity, resulting in loss of membrane integrity at the cellular level. The induction of late embryogenesis abundant proteins (LEAPs) is considered an essential component of desiccation tolerance strategy in so-called resurrection plants. This heterogeneous group of hydrophilic, non-globular proteins is characterized by a high structural plasticity that allows them to adopt a random conformation in aqueous solutions that transforms into α-helices during dehydration [1]. Therefore, LEAPs can interact with various ligands and partners, including ion sequestration and stabilization of membranes and enzymes during freezing or drying [2]. Our new transcriptome database of an endemic resurrection species Ramonda serbica allowed us to identify 153 members of the LEA gene family. LEAPs of this sample data have an average primary sequence similarity and identity of 10% and 6%, respectively, but with a high variance (141 and 108), which means that the sample proteins can be classified based on domain homology. The averaging is based on multiple sequence alignment and the variance is estimated using pairwise sequence alignment scores. Accordingly, all identified LEAPs were clustered into six groups based on protein families (PFAM). Among these groups, LEAPs differ significantly in their secondary structure, disorder propensity and aggregation potential. Furthermore, we built homology models using Protein Data Bank structure information as templates. For each group, an ensemble of superimposed 3D homology models was analyzed. The information obtained from the representative structural models is key to understanding the function of LEAPs and the regulation of their intrinsic structural disorder-to-order transition during desiccation. This will pave the way for the identification of LEAPs endogenous partners and their targets in the cell and provide further insights into the protective mechanisms of desiccation tolerance.",
journal = "Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5",
title = "In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1836"
}

Stevanović, S.,& Vidović, M.. (2021). In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship. in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5.
https://hdl.handle.net/21.15107/rcub_imagine_1836

Stevanović S, Vidović M. In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship. in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5. 2021;.
https://hdl.handle.net/21.15107/rcub_imagine_1836 .

Stevanović, Strahinja, Vidović, Marija, "In silico structural survey of newly identified late embryogenesis abundant proteins (LEAPs) from Ramonda serbica and their structure - function relationship" in Virtual symposium celebrating the 50th anniversary of the Protein Data Bank, May 4–5 (2021),
https://hdl.handle.net/21.15107/rcub_imagine_1836 .

TY  - CONF
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
AU  - Kilibarda, Nataša
AU  - Milić Komić, Sonja
AU  - Radosavljevic, Jelena
AU  - Vidović, Marija
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1882
AB  - Endemic plant species, Ramonda serbica is a resurrection plant that can tolerate extreme
dehydration (desiccation, loss of 95% of cellular water) even over months. The
accumulation of late embryogenesis abundant proteins (LEAPs) is a crucial step in the
mechanism of desiccation tolerance. The role of LEAPs is not completely resolved, but
they are accepted as intrinsically disordered proteins (IDPs). Based on previously
established de novo transcriptome database of R. serbica leaves we identify around 160
members of LEA gene family. Identified LEAPs were classified into six groups: LEA 1-5
and seed maturation proteins (SMPs) according to protein family (Pfam) database. Based
on multiple sequence alignment, secondary structure prediction and 3D structure modeling,
we conducted LEA protein structure analysis. We showed that more than 50% of identified
LEAPs exhibited a high propensity to form α-helices. As predicted by several
bioinformatic tools, more than 70% of identified LEAPs were found to be highly
disordered. Thus, these proteins are predicted to be disordered in solution, but they acquire
a secondary, predominantly α-helical structure during drying, in contrast to globular
proteins, which most often causes the loss of structure upon dehydration. By using
molecular dynamic simulations, we identified the most favorable conformations of
representative LEAPs and we have studied conformational transitions driven by the water
scarcity. Structural characterization of LEAPs is a key to understand their function and
regulation of their intrinsic structural disorder-to-order transition during desiccation as a
requirement for biological function, in order to promote development of new therapeutic
strategies in neurodegenerative disorders, cell preservation technology and the
improvement of crop drought tolerance.
PB  - Belgrade : Serbian Biochemical Society
C3  - Biochemical Insights into Molecular Mechanisms
T1  - Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves
SP  - 117
SP  - 118
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1882
ER  - 

@conference{
author = "Pantelić, Ana and Stevanović, Strahinja and Kilibarda, Nataša and Milić Komić, Sonja and Radosavljevic, Jelena and Vidović, Marija",
year = "2021",
abstract = "Endemic plant species, Ramonda serbica is a resurrection plant that can tolerate extreme
dehydration (desiccation, loss of 95% of cellular water) even over months. The
accumulation of late embryogenesis abundant proteins (LEAPs) is a crucial step in the
mechanism of desiccation tolerance. The role of LEAPs is not completely resolved, but
they are accepted as intrinsically disordered proteins (IDPs). Based on previously
established de novo transcriptome database of R. serbica leaves we identify around 160
members of LEA gene family. Identified LEAPs were classified into six groups: LEA 1-5
and seed maturation proteins (SMPs) according to protein family (Pfam) database. Based
on multiple sequence alignment, secondary structure prediction and 3D structure modeling,
we conducted LEA protein structure analysis. We showed that more than 50% of identified
LEAPs exhibited a high propensity to form α-helices. As predicted by several
bioinformatic tools, more than 70% of identified LEAPs were found to be highly
disordered. Thus, these proteins are predicted to be disordered in solution, but they acquire
a secondary, predominantly α-helical structure during drying, in contrast to globular
proteins, which most often causes the loss of structure upon dehydration. By using
molecular dynamic simulations, we identified the most favorable conformations of
representative LEAPs and we have studied conformational transitions driven by the water
scarcity. Structural characterization of LEAPs is a key to understand their function and
regulation of their intrinsic structural disorder-to-order transition during desiccation as a
requirement for biological function, in order to promote development of new therapeutic
strategies in neurodegenerative disorders, cell preservation technology and the
improvement of crop drought tolerance.",
publisher = "Belgrade : Serbian Biochemical Society",
journal = "Biochemical Insights into Molecular Mechanisms",
title = "Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves",
pages = "117-118",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1882"
}

Pantelić, A., Stevanović, S., Kilibarda, N., Milić Komić, S., Radosavljevic, J.,& Vidović, M.. (2021). Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves. in Biochemical Insights into Molecular Mechanisms
Belgrade : Serbian Biochemical Society., 117.
https://hdl.handle.net/21.15107/rcub_imagine_1882

Pantelić A, Stevanović S, Kilibarda N, Milić Komić S, Radosavljevic J, Vidović M. Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves. in Biochemical Insights into Molecular Mechanisms. 2021;:117.
https://hdl.handle.net/21.15107/rcub_imagine_1882 .

Pantelić, Ana, Stevanović, Strahinja, Kilibarda, Nataša, Milić Komić, Sonja, Radosavljevic, Jelena, Vidović, Marija, "Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves" in Biochemical Insights into Molecular Mechanisms (2021):117,
https://hdl.handle.net/21.15107/rcub_imagine_1882 .

TY  - CONF
AU  - Vidović, Marija
AU  - Stevanović, Strahinja
AU  - Franchin, Cinzia
AU  - Battisti, Ilaria
AU  - Arrigoni, Giorgio
AU  - Masi, Antonio
AU  - Veljović Jovanović, Sonja
PY  - 2021
UR  - https://inppo.org/inppo2020/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1835
AB  - Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.
PB  - International Plant Proteomics Organization
C3  - The Fourth Conference of the International Plant Proteomics Organization
T1  - Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves
EP  - 44
SP  - 43
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1835
ER  - 

@conference{
author = "Vidović, Marija and Stevanović, Strahinja and Franchin, Cinzia and Battisti, Ilaria and Arrigoni, Giorgio and Masi, Antonio and Veljović Jovanović, Sonja",
year = "2021",
abstract = "Resurrection plant Ramonda serbica Panc. survives desiccation for a long period and fully recovers metabolic functions already within one day upon watering [1]. Besides osmotic stress, desiccation provokes the accelerated generation of reactive oxygen species. The aim of our study was obtaining more insight into the mechanisms of desiccation tolerance in R. serbica by TMT labelled comparative quantitative proteomics of hydrated (HL) and desiccated leaves (DL). After de novo transcriptome analysis, 189456 transcripts with 189003 unigenes were annotated with seven common databases. Proteomic analysis allowed for the relative quantification of 895 different protein groups, 321 with a statistically significant difference in abundance between FL and DL. Among them, 25% referred to chloroplast and almost the same percentage were associated with desiccation and oxidative stress. Almost all differentially abundant proteins related to photosynthetic processes were down-regulated in DL, while those required for protein translation were more abundant in HL. Within differentially abundant proteins involved in antioxidative defence, the levels of enzymes involved in ascorbate-glutathione cycle, peroxiredoxins, Fe and Mn superoxide dismutase (SOD) were all reduced in DL, while germin-like proteins, three Cu/Zn SOD isoforms and polyphenol oxidases were more abundant in DL compared with HL. The protein family with the highest number of members showing the greatest accumulation upon desiccation comprised twenty different late embryogenesis abundant proteins (LEAPs), similarly as found by differential transcriptomic analysis. Taken together, our results imply a key role of LEAPs and Cu/Zn SOD in protective mechanism against desiccation in R. serbica, that may have significant implications on drought-related studies of crops grown in arid areas. This work was supported by the Science Fund of the Republic of Serbia (PROMIS project LEAPSyn-SCI, grant number 6039663). M.V. wishes to acknowledge the support of COST Action BM1405 for approving STSM in Padua during 2017 and 2018.",
publisher = "International Plant Proteomics Organization",
journal = "The Fourth Conference of the International Plant Proteomics Organization",
title = "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves",
pages = "44-43",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1835"
}

Vidović, M., Stevanović, S., Franchin, C., Battisti, I., Arrigoni, G., Masi, A.,& Veljović Jovanović, S.. (2021). Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization
International Plant Proteomics Organization., 43-44.
https://hdl.handle.net/21.15107/rcub_imagine_1835

Vidović M, Stevanović S, Franchin C, Battisti I, Arrigoni G, Masi A, Veljović Jovanović S. Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves. in The Fourth Conference of the International Plant Proteomics Organization. 2021;:43-44.
https://hdl.handle.net/21.15107/rcub_imagine_1835 .

Vidović, Marija, Stevanović, Strahinja, Franchin, Cinzia, Battisti, Ilaria, Arrigoni, Giorgio, Masi, Antonio, Veljović Jovanović, Sonja, "Twenty different late embryogenesis abundant proteins (LEAPs) accumulate in desiccated Ramonda serbica leaves" in The Fourth Conference of the International Plant Proteomics Organization (2021):43-44,
https://hdl.handle.net/21.15107/rcub_imagine_1835 .

TY  - GEN
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
AU  - Kilibarda, Nataša
AU  - Vidović, Marija
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1852
AB  - Resurrection plant Ramonda serbica Panc. survives
desiccation for a long period and fully recovers
metabolic functions already within one day upon
watering. Desiccation (extreme dehydration) induces protein
unfolding and aggregation, destabilization or loss of
cellular membrane integrity. Besides, desiccation
provokes the accelerated generation of reactive
oxygen species.
HL
DL

Aim: To identify Late Embryogenesis Abundant Proteins
(LEAPs) that contribute to desiccation tolerance in
R. serbica by comparative transcriptomics of
hydrated (HL) and desiccated leaves (DL).
PB  - Belgrade BioInformatics
T2  - Belgrade BioInformatics Conference 2021
T1  - De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1852
ER  - 

@misc{
author = "Pantelić, Ana and Stevanović, Strahinja and Kilibarda, Nataša and Vidović, Marija",
year = "2021",
abstract = "Resurrection plant Ramonda serbica Panc. survives
desiccation for a long period and fully recovers
metabolic functions already within one day upon
watering. Desiccation (extreme dehydration) induces protein
unfolding and aggregation, destabilization or loss of
cellular membrane integrity. Besides, desiccation
provokes the accelerated generation of reactive
oxygen species.
HL
DL

Aim: To identify Late Embryogenesis Abundant Proteins
(LEAPs) that contribute to desiccation tolerance in
R. serbica by comparative transcriptomics of
hydrated (HL) and desiccated leaves (DL).",
publisher = "Belgrade BioInformatics",
journal = "Belgrade BioInformatics Conference 2021",
title = "De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1852"
}

Pantelić, A., Stevanović, S., Kilibarda, N.,& Vidović, M.. (2021). De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins. in Belgrade BioInformatics Conference 2021
Belgrade BioInformatics..
https://hdl.handle.net/21.15107/rcub_imagine_1852

Pantelić A, Stevanović S, Kilibarda N, Vidović M. De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins. in Belgrade BioInformatics Conference 2021. 2021;.
https://hdl.handle.net/21.15107/rcub_imagine_1852 .

Pantelić, Ana, Stevanović, Strahinja, Kilibarda, Nataša, Vidović, Marija, "De Novo Transcriptome Sequencing of Ramonda serbica : Identification of Late Embryogenesis Abundant Proteins" in Belgrade BioInformatics Conference 2021 (2021),
https://hdl.handle.net/21.15107/rcub_imagine_1852 .

TY  - CONF
AU  - Vidović, Marija
AU  - Pantelić, Ana
AU  - Stevanović, Strahinja
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1881
AB  - Ramonda serbica is an endemic and resurrection plant species that can survive
extreme dehydration even over months. Desiccation (loss of >95% of cellular water) leads to
protein denaturation, aggregation, and degradation and impairs membrane lipid fluidity, resulting in
loss of membrane integrity at the cellular level. The induction of late embryogenesis abundant
proteins (LEAPs) is considered an essential component of desiccation tolerance strategy in so-called
resurrection plants. This heterogeneous group of anhydrobiosis-related intrinsically
disordered proteins (IDPs) is characterized by high structural plasticity enabling them to interact
with various ligands and partners, including ion sequestration and stabilization of membranes and
enzymes during freezing or drying. the aim of our research is to assess the potential of selected
RsLEAPs to inhibit the aggregation of α-synuclein, paving the way for new therapeutic
strategies against neurodegenerative disorders, such as Parkinson’s disease.
Our new transcriptome database of R. serbica leaves allowed us to identify around 165
members of LEA protein family. Based on multiple sequence alignment, secondary structure
prediction and 3D structure modelling we classified identified LEAPs into six groups
(according to the Pfam database) and showed that more than 50% of identified LEAPs
exhibited a high propensity to form α-helices. As predicted by several bioinformatic tools,
more than 70% of identified LEAPs were found to be highly disordered. By using molecular
dynamic simulations, we identified the most favourable conformations of representative
LEAPs and showed the loss of the secondary, α-helical structure in water, in contrast to
globular proteins.
Structural characterization of LEAPs is a key to understand their function and
regulation of their intrinsic structural disorder-to-order transition during desiccation. These
findings will promote transformative advancements in various fields, such as the
development of new strategies in neurodegenerative disorders, cell preservation technology
and the improvement of crop drought tolerance.
AB  - Ramonda serbica endemska vrsta, i biljka vaskrsnica, sposobna da preživi u uslovima
ekstremne dehidratacije tokom perioda dužeg od mesec dana. Desikacija (gubitak preko 95
% vode u ćeliji) dovodi do denaturacije, agregacije i degradacije proteina, i utiče na fluidnost
membrana, što finalno dovodi do gubitka integriteta ćelije. Prisustvo proteina zastupljenih u
kasnoj fazi embriogeneze (late embryogenesis abundant proteins – LEAPs) se smatra esencijalnim
delom strategije tolerancije na desikaciju kod vaskrsnica. Ovu heterogenu grupu prirodno neuređenih
proteina, povezanih sa anhidrobiozom, odlikuje visoka strukturna plastičnost koja im omogućava
interakciju sa brojnim ligandima i partnerima. LEA proteini su uključeni u heliranje jona, stabilizaciju
membrana i enzima tokom zamrzavanja ili suše. Cilj našeg istraživanja je procena potencijala
izabranog LEA proteina iz ramonde da inhibira agregaciju α-sinukleina, otvarajući put ka razvoju
novih terapija za lečenje neurodegenerativnih poremećaja poput Parkinskonove bolesti.
Analiziranjem transkriptoma listova R. serbica i formiranjem baze podataka
identifikovano je oko 165 proteina koji pripadaju LEA proteinskoj familiji. Na osnovu
višestrukog poravnjanja aminokiselinskih sekvenci, predviđanja sekundarne strukture i 3D
strukturnog modelinga, identifikovani LEA proteini su podeljeni u šest grupa (prema Pfam
bazi podataka) i pokazano je sa velikom verovatnoćom da je više od 50 % LEA proteina u
mogućnosti da formira α-helikse. Pomoću nekoliko bioinformatičkih alata predviđeno je da
više od 70 % identifikovanih LEA proteina formira visoko neuređenu strukturu. Korišćenjem
simulacije molekularne dinamike, identifikovane su najpovoljnije konformacije
reprezentativnih LEA proteina. Tom prilikom je kod LEA proteina uočen gubitak sekundarne
α-heliksne strukture u vodi, za razliku od globularnih proteina kada je ova struktura
favorizovana.
Strukturna karakterizacija LEA proteina je ključna za razumevanje njihove funkcije i
regulaciju njihovog prelaska iz neuređene u uređenu konformaciju tokom desikacije. Ova
saznanja bi trebalo da omoguće značajna napredovanja na različitim poljima, kao što je
razvoj novih strategija u borbi protiv neurodegenerativnih poremećaja, tehnologija čuvanja
zamrznutih ćelija, kao i na povećanje otpornosti useva na sušu.
PB  - Beograd : Savez farmaceutskih udruženja Srbije
C3  - Archives of Pharmacy -  2nd Scientific symposium SFUS
T1  - Structural characterisation of Late Embryogenesis Abundant Proteins from Ramonda Serbica: potential to inhibit α-synuclein aggregation
T1  - Strukturna karakterizacija proteina zastupljenih u kasnoj fazi embriogeneze iz biljke Ramonda Serbica : Potencijalni inhibitor agregacije  α‐ sinukleina
EP  - 31
IS  - Suppl. 5
SP  - 30
VL  - 71
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1881
ER  - 

@conference{
author = "Vidović, Marija and Pantelić, Ana and Stevanović, Strahinja",
year = "2021",
abstract = "Ramonda serbica is an endemic and resurrection plant species that can survive
extreme dehydration even over months. Desiccation (loss of >95% of cellular water) leads to
protein denaturation, aggregation, and degradation and impairs membrane lipid fluidity, resulting in
loss of membrane integrity at the cellular level. The induction of late embryogenesis abundant
proteins (LEAPs) is considered an essential component of desiccation tolerance strategy in so-called
resurrection plants. This heterogeneous group of anhydrobiosis-related intrinsically
disordered proteins (IDPs) is characterized by high structural plasticity enabling them to interact
with various ligands and partners, including ion sequestration and stabilization of membranes and
enzymes during freezing or drying. the aim of our research is to assess the potential of selected
RsLEAPs to inhibit the aggregation of α-synuclein, paving the way for new therapeutic
strategies against neurodegenerative disorders, such as Parkinson’s disease.
Our new transcriptome database of R. serbica leaves allowed us to identify around 165
members of LEA protein family. Based on multiple sequence alignment, secondary structure
prediction and 3D structure modelling we classified identified LEAPs into six groups
(according to the Pfam database) and showed that more than 50% of identified LEAPs
exhibited a high propensity to form α-helices. As predicted by several bioinformatic tools,
more than 70% of identified LEAPs were found to be highly disordered. By using molecular
dynamic simulations, we identified the most favourable conformations of representative
LEAPs and showed the loss of the secondary, α-helical structure in water, in contrast to
globular proteins.
Structural characterization of LEAPs is a key to understand their function and
regulation of their intrinsic structural disorder-to-order transition during desiccation. These
findings will promote transformative advancements in various fields, such as the
development of new strategies in neurodegenerative disorders, cell preservation technology
and the improvement of crop drought tolerance., Ramonda serbica endemska vrsta, i biljka vaskrsnica, sposobna da preživi u uslovima
ekstremne dehidratacije tokom perioda dužeg od mesec dana. Desikacija (gubitak preko 95
% vode u ćeliji) dovodi do denaturacije, agregacije i degradacije proteina, i utiče na fluidnost
membrana, što finalno dovodi do gubitka integriteta ćelije. Prisustvo proteina zastupljenih u
kasnoj fazi embriogeneze (late embryogenesis abundant proteins – LEAPs) se smatra esencijalnim
delom strategije tolerancije na desikaciju kod vaskrsnica. Ovu heterogenu grupu prirodno neuređenih
proteina, povezanih sa anhidrobiozom, odlikuje visoka strukturna plastičnost koja im omogućava
interakciju sa brojnim ligandima i partnerima. LEA proteini su uključeni u heliranje jona, stabilizaciju
membrana i enzima tokom zamrzavanja ili suše. Cilj našeg istraživanja je procena potencijala
izabranog LEA proteina iz ramonde da inhibira agregaciju α-sinukleina, otvarajući put ka razvoju
novih terapija za lečenje neurodegenerativnih poremećaja poput Parkinskonove bolesti.
Analiziranjem transkriptoma listova R. serbica i formiranjem baze podataka
identifikovano je oko 165 proteina koji pripadaju LEA proteinskoj familiji. Na osnovu
višestrukog poravnjanja aminokiselinskih sekvenci, predviđanja sekundarne strukture i 3D
strukturnog modelinga, identifikovani LEA proteini su podeljeni u šest grupa (prema Pfam
bazi podataka) i pokazano je sa velikom verovatnoćom da je više od 50 % LEA proteina u
mogućnosti da formira α-helikse. Pomoću nekoliko bioinformatičkih alata predviđeno je da
više od 70 % identifikovanih LEA proteina formira visoko neuređenu strukturu. Korišćenjem
simulacije molekularne dinamike, identifikovane su najpovoljnije konformacije
reprezentativnih LEA proteina. Tom prilikom je kod LEA proteina uočen gubitak sekundarne
α-heliksne strukture u vodi, za razliku od globularnih proteina kada je ova struktura
favorizovana.
Strukturna karakterizacija LEA proteina je ključna za razumevanje njihove funkcije i
regulaciju njihovog prelaska iz neuređene u uređenu konformaciju tokom desikacije. Ova
saznanja bi trebalo da omoguće značajna napredovanja na različitim poljima, kao što je
razvoj novih strategija u borbi protiv neurodegenerativnih poremećaja, tehnologija čuvanja
zamrznutih ćelija, kao i na povećanje otpornosti useva na sušu.",
publisher = "Beograd : Savez farmaceutskih udruženja Srbije",
journal = "Archives of Pharmacy -  2nd Scientific symposium SFUS",
title = "Structural characterisation of Late Embryogenesis Abundant Proteins from Ramonda Serbica: potential to inhibit α-synuclein aggregation, Strukturna karakterizacija proteina zastupljenih u kasnoj fazi embriogeneze iz biljke Ramonda Serbica : Potencijalni inhibitor agregacije  α‐ sinukleina",
pages = "31-30",
number = "Suppl. 5",
volume = "71",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1881"
}

Vidović, M., Pantelić, A.,& Stevanović, S.. (2021). Structural characterisation of Late Embryogenesis Abundant Proteins from Ramonda Serbica: potential to inhibit α-synuclein aggregation. in Archives of Pharmacy -  2nd Scientific symposium SFUS
Beograd : Savez farmaceutskih udruženja Srbije., 71(Suppl. 5), 30-31.
https://hdl.handle.net/21.15107/rcub_imagine_1881

Vidović M, Pantelić A, Stevanović S. Structural characterisation of Late Embryogenesis Abundant Proteins from Ramonda Serbica: potential to inhibit α-synuclein aggregation. in Archives of Pharmacy -  2nd Scientific symposium SFUS. 2021;71(Suppl. 5):30-31.
https://hdl.handle.net/21.15107/rcub_imagine_1881 .

Vidović, Marija, Pantelić, Ana, Stevanović, Strahinja, "Structural characterisation of Late Embryogenesis Abundant Proteins from Ramonda Serbica: potential to inhibit α-synuclein aggregation" in Archives of Pharmacy -  2nd Scientific symposium SFUS, 71, no. Suppl. 5 (2021):30-31,
https://hdl.handle.net/21.15107/rcub_imagine_1881 .

TY  - CONF
AU  - Vidović, Marija
AU  - Stevanović, Strahinja
AU  - Veljović-Jovanović, Sonja
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1834
AB  - Ramonda serbica Panc. is a resurrection plant that can survive a long period of severe dehydration-desiccation. Desiccation induces cellular membrane integrity loss, protein aggregation, and denaturation, as well as accelerated generation of reactive oxygen species. However, R. serbica can fully recover its metabolic functions already one day upon watering [1]. The aim of our study was to obtain more insight into the desiccation tolerance mechanisms by differential de novo transcriptomics of hydrated (HL) and desiccated leaves (DL). For R. serbica transcriptome construction, the total high-quality RNA from HL and DL was extracted according to our previously optimised protocol [2]. Highly purified cDNA libraries were sequenced on an Illumina Hi-Seq platform. The ambiguous nucleotides, adapter sequences, and low-quality sequences were trimmed, and the quality of the reads was checked before and after the trimming. In total, 39608813 (with Q30=94%) and 37482969 (with Q30=94.1%) clean reads were obtained in HL and DL, respectively, and used to perform transcriptome assembly by Trinity software. After removing the redundancy, 189456 transcripts with 189003 unigenes were obtained (32.6% with the length between 500-1kbp).Comparative analysis revealed that a large portion of R. serbica sequences (49.1%) was similar to sequences found in the genome of another resurrection plant Boea hygrometrica. Furthermore, among obtained unigenes, 64.6% and 42.3% were annotated by NCBI non-redundant protein and nucleotide sequences database (db), 23% by PFAM db, 22.5% by Clusters of Orthologous Groups of proteins db, 48.02% by Swiss-Prot db, 23 % KEGG db and 13.73 by Gene Ontology db. The majority of annotated genes were associated with translation, ribosomal structure, posttranslational modifications, protein turnover, signalling pathways and cytoskeleton and encoded chaperonins and late embryogenesis abundant (LEA) proteins. Aiming to provide a list of candidates involved in the desiccation tolerance in R. serbica we analysed differentially expressed genes in HL and DL. Genes associated with transmembrane transport, reproduction, cell proliferation, and protein folding were up-regulated in HL compared with DL. On the other hand, genes encoding proteins involved in cell wall architecture, LEA proteins and antioxidative defence were up-regulated in DL.
C3  - Biologia Serbica
T1  - De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance
EP  - 76
IS  - 1 (spec. ed.)
SP  - 75
VL  - 43
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1834
ER  - 

@conference{
author = "Vidović, Marija and Stevanović, Strahinja and Veljović-Jovanović, Sonja",
year = "2021",
abstract = "Ramonda serbica Panc. is a resurrection plant that can survive a long period of severe dehydration-desiccation. Desiccation induces cellular membrane integrity loss, protein aggregation, and denaturation, as well as accelerated generation of reactive oxygen species. However, R. serbica can fully recover its metabolic functions already one day upon watering [1]. The aim of our study was to obtain more insight into the desiccation tolerance mechanisms by differential de novo transcriptomics of hydrated (HL) and desiccated leaves (DL). For R. serbica transcriptome construction, the total high-quality RNA from HL and DL was extracted according to our previously optimised protocol [2]. Highly purified cDNA libraries were sequenced on an Illumina Hi-Seq platform. The ambiguous nucleotides, adapter sequences, and low-quality sequences were trimmed, and the quality of the reads was checked before and after the trimming. In total, 39608813 (with Q30=94%) and 37482969 (with Q30=94.1%) clean reads were obtained in HL and DL, respectively, and used to perform transcriptome assembly by Trinity software. After removing the redundancy, 189456 transcripts with 189003 unigenes were obtained (32.6% with the length between 500-1kbp).Comparative analysis revealed that a large portion of R. serbica sequences (49.1%) was similar to sequences found in the genome of another resurrection plant Boea hygrometrica. Furthermore, among obtained unigenes, 64.6% and 42.3% were annotated by NCBI non-redundant protein and nucleotide sequences database (db), 23% by PFAM db, 22.5% by Clusters of Orthologous Groups of proteins db, 48.02% by Swiss-Prot db, 23 % KEGG db and 13.73 by Gene Ontology db. The majority of annotated genes were associated with translation, ribosomal structure, posttranslational modifications, protein turnover, signalling pathways and cytoskeleton and encoded chaperonins and late embryogenesis abundant (LEA) proteins. Aiming to provide a list of candidates involved in the desiccation tolerance in R. serbica we analysed differentially expressed genes in HL and DL. Genes associated with transmembrane transport, reproduction, cell proliferation, and protein folding were up-regulated in HL compared with DL. On the other hand, genes encoding proteins involved in cell wall architecture, LEA proteins and antioxidative defence were up-regulated in DL.",
journal = "Biologia Serbica",
title = "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance",
pages = "76-75",
number = "1 (spec. ed.)",
volume = "43",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1834"
}

Vidović, M., Stevanović, S.,& Veljović-Jovanović, S.. (2021). De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance. in Biologia Serbica, 43(1 (spec. ed.)), 75-76.
https://hdl.handle.net/21.15107/rcub_imagine_1834

Vidović M, Stevanović S, Veljović-Jovanović S. De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance. in Biologia Serbica. 2021;43(1 (spec. ed.)):75-76.
https://hdl.handle.net/21.15107/rcub_imagine_1834 .

Vidović, Marija, Stevanović, Strahinja, Veljović-Jovanović, Sonja, "De Novo Transcriptome Sequencing of Ramonda serbica: Identification of the Candidate Genes Involved in the Desiccation Tolerance" in Biologia Serbica, 43, no. 1 (spec. ed.) (2021):75-76,
https://hdl.handle.net/21.15107/rcub_imagine_1834 .

TY  - CONF
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1877
AB  - An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation,
aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane
integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants
are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related
intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into
compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding,
ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming
intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells
during desiccation.
Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica
by integrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs
were classification into six groups according to Protein family (PFAM) database and the most populated
group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we
showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence
length is predicted to form α-helical structure). This implies that charged residues might be exposed to the
solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in
the cell. In addition, as predicted by several bioinformatics tools, more than 70% of identified LEAPs were
found to be highly disordered. Structural characterization of LEAPs is a key to understand their function
and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings
will promote transformative advancements in various fields, such as the development of new strategies in
neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.
PB  - Novi Sad : Faculty of Sciences, Department of Biology and Ecology
C3  - Biologia Serbica
T1  - De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins
IS  - 1 (Special Edition)
SP  - 65
VL  - 43
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1877
ER  - 

@conference{
year = "2021",
abstract = "An extreme loss of cellular water or desiccation (5-10% of relative water content) leads to protein denaturation,
aggregation and degradation, and affects the fluidity of membrane lipids resulting in loss of membrane
integrity [1]. The essential constituents of vegetative desiccation tolerance in so-called resurrection plants
are late embryogenesis abundant proteins (LEAPs). This heterogeneous group of anhydrobiosis-related
intrinsically disordered proteins forms mostly random conformation when fully hydrated, turning into
compact α-helices during desiccation [2]. Based on in vitro studies, LEAPs can be involved in water binding,
ion sequestration, stabilization of both membrane and enzymes during freezing or drying, while by forming
intracellular proteinaceous condensates they increase structural integrity and intracellular viscosity of cells
during desiccation.
Here, we identify 164 members of LEA gene family in endemic and relict resurrection species Ramonda serbica
by integrating previously done de novo transcriptome and homologues protein motifs. Identified LEAPs
were classification into six groups according to Protein family (PFAM) database and the most populated
group was LEA4 containing 47% of total identified LEAPs. By using four secondary structure predictors, we
showed that this group exhibited a high propensity to form amphipathic α-helices (81% of total sequence
length is predicted to form α-helical structure). This implies that charged residues might be exposed to the
solvent, while hydrophobic amino acids might interact with lipid bilayers or with other target proteins in
the cell. In addition, as predicted by several bioinformatics tools, more than 70% of identified LEAPs were
found to be highly disordered. Structural characterization of LEAPs is a key to understand their function
and regulation of their intrinsic structural disorder-to-order transition during desiccation. These findings
will promote transformative advancements in various fields, such as the development of new strategies in
neurodegenerative disorders, cell preservation technology and the improvement of crop drought tolerance.",
publisher = "Novi Sad : Faculty of Sciences, Department of Biology and Ecology",
journal = "Biologia Serbica",
title = "De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins",
number = "1 (Special Edition)",
pages = "65",
volume = "43",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1877"
}

(2021). De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins. in Biologia Serbica
Novi Sad : Faculty of Sciences, Department of Biology and Ecology., 43(1 (Special Edition)), 65.
https://hdl.handle.net/21.15107/rcub_imagine_1877

De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins. in Biologia Serbica. 2021;43(1 (Special Edition)):65.
https://hdl.handle.net/21.15107/rcub_imagine_1877 .

"De Novo Transcriptome Sequencing of Ramonda serbica Identification of Late Embryogenesis Abundant Proteins" in Biologia Serbica, 43, no. 1 (Special Edition) (2021):65,
https://hdl.handle.net/21.15107/rcub_imagine_1877 .