Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves
Аутори
Pantelic, AnaStevanovic, Strahinja
Kilibarda, Nataša
Milić Komić, Sonja
Radosavljevic, Jelena
Vidović, Marija
Конференцијски 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 LEAPs were fo...und 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-, 2021, 117-118Издавач:
- 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 multidisciplinarna istraživanjaTY - CONF AU - Pantelic, Ana AU - Stevanovic, Strahinja AU - Kilibarda, Nataša AU - Milić Komić, Sonja AU - Radosavljevic, Jelena AU - Vidović, Marija PY - 2021 UR - http://rimsi.imsi.bg.ac.rs/handle/123456789/3083 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, 2021, 117- T1 - Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves EP - 118 SP - 117 UR - https://hdl.handle.net/21.15107/rcub_rimsi_3083 ER -
@conference{ author = "Pantelic, Ana and Stevanovic, 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, 2021, 117-", title = "Characterization of the late embryogenesis abundant (LEA) proteins family in hydrated and desiccated Ramonda serbica Panc. leaves", pages = "118-117", url = "https://hdl.handle.net/21.15107/rcub_rimsi_3083" }
Pantelic, A., Stevanovic, 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, 2021, 117- Belgrade : Serbian Biochemical Society., 117-118. https://hdl.handle.net/21.15107/rcub_rimsi_3083
Pantelic A, Stevanovic 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-. 2021;:117-118. https://hdl.handle.net/21.15107/rcub_rimsi_3083 .
Pantelic, Ana, Stevanovic, 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- (2021):117-118, https://hdl.handle.net/21.15107/rcub_rimsi_3083 .