Two contrasting late embryogenesis abounded protein family groups of Ramonda serbica Panc.
Autori
Pantelić, AnaStevanović, Strahinja
Milić Komić, Sonja
Kilibarda, Nataša
Vidović, Marija
Ostala autorstva
Morić, IvanaĐorđević, Valentina
Konferencijski prilog (Objavljena verzija)
,
© 2023 Institute of Molecular Genetics and Genetic Engineering, University of Belgrade
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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 hyd...rophobic 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.
Ključne reči:
LEA proteins / secondary structure prediction / IDPs / resurrection plantsIzvor:
4th Belgrade Bioinformatics Conference, 2023, 4, 68-68Izdavač:
- Belgrade : Institute of molecular genetics and genetic engineering
Finansiranje / projekti:
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200042 (Univerzitet u Beogradu, Institut za molekularnu genetiku i genetičko inženjerstvo) (RS-MESTD-inst-2020-200042)
- LEAPSyn-SCI - Late Embryogenesis Abundant Proteins: Structural Characterisation and Interaction With Α-Synuclein (RS-ScienceFundRS-Promis-6039663)
Napomena:
- Book of abstract: 4th Belgrade Bioinformatics Conference, June 19-23, 2023
Institucija/grupa
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 .