Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves
Аутори
Pantelić, AnaStevanović, Strahinja
Kilibarda, Nataša
Milić Komić, Sonja
Radosavljevic, Jelena
Vidović, Marija
Остала ауторства
Spasojević, IvanaКонференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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 LE...APs 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.
Кључне речи:
resurrection plants / desiccation tolerance / intrinsically disordered proteins / molecular dynamic simulations / α-helical structureИзвор:
Biochemical Insights into Molecular Mechanisms, 2021, 117-Издавач:
- Belgrade : Serbian Biochemical Society
Финансирање / пројекти:
- LEAPSyn-SCI - Late Embryogenesis Abundant Proteins: Structural Characterisation and Interaction With Α-Synuclein (RS-ScienceFundRS-Promis-6039663)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200042 (Универзитет у Београду, Институт за молекуларну генетику и генетичко инжењерство) (RS-MESTD-inst-2020-200042)
Напомена:
- Serbian Biochemical Society, 10th Conference, Kragujevac, Serbia, 24.09.2021
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 .