Radosavljevic, Jelena

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  • Radosavljevic, Jelena (1)
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Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves

Pantelić, Ana; Stevanović, Strahinja; Kilibarda, Nataša; Milić Komić, Sonja; Radosavljevic, Jelena; Vidović, Marija

(Belgrade : Serbian Biochemical Society, 2021)

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 .