Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization
Autori
Pantelic, AnaStevanovic, Strahinja
Milić, Dejana
Milić Komić, Sonja
Kilibarda, Nataša
Vidović, Marija
Konferencijski prilog (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
An ancient resurrection plant Ramonda serbica Panc. is able to survive a long desiccation period and reestablish metabolic activity upon watering. A hallmark of desiccation tolerance in the resurrection species is the accumulation of protective late embryogenesis abundant proteins (LEAPs). These intrinsically disordered proteins (IDPs) may stabilize the correct structure of proteins and membranes during cellular dehydration. The aim of our study was to assess LEA genes’ expression levels in hydrated (HL) and desiccated leaves (DL) and to identify, characterise, and estimate the potential role of R. serbica LEAPs in desiccation tolerance. In total, 318 LEAPs from HL and DL were identified and classified into the seven LEA protein family groups ranging from LEA1-LEA5, seed maturation proteins (SMPs), and dehydrins (DEH). Analysis of the physicochemical properties, motif architecture, secondary structure, homology, and phylogenetic relationships demonstrated that R. serbica LEAPs greatly ...differed among the LEA family groups. The most abundant LEA2 proteins (mostly downregulated upon desiccation) exhibited lower hydrophilicity and propensity to fold into organised globular domains. Oppositely, hydrophilic LEA4 proteins tended to form amphipathic, A-type, α-helices. Most of desiccation-upregulated LEA genes encoded highly disordered DEH1, LEA1, LEA4.2, and LEA4.3 proteins. While dehydrins might chelate metals and bind DNA under water deficit, other ID LEAPs (e.g. LEA1, LEA3, LEA4) might participate in forming intracellular proteinaceous condensates or adopt amphipathic α-helical conformation, enabling them to stabilise desiccation-sensitive proteins and membranes. Taken together, possible functions of LEAPs are discussed with significant implications on drought tolerance improvement of crops grown in arid areas.
Ključne reči:
3D protein structure modelling / de novo transcriptome assembly / intrinsically disordered proteins / liquid-liquid phase separation / secondary structure predictionIzvor:
Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83-, 2022, 95-Izdavač:
- Serbian Plant Physiology Society
- Institute for Biological Research “Siniša Stanković” – National Institute of Republic of Serbia, University of Belgrade
- Faculty of Biology, University of Belgrade
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)
Institucija/grupa
Institut za multidisciplinarna istraživanjaTY - CONF AU - Pantelic, Ana AU - Stevanovic, Strahinja AU - Milić, Dejana AU - Milić Komić, Sonja AU - Kilibarda, Nataša AU - Vidović, Marija PY - 2022 UR - http://rimsi.imsi.bg.ac.rs/handle/123456789/3085 AB - An ancient resurrection plant Ramonda serbica Panc. is able to survive a long desiccation period and reestablish metabolic activity upon watering. A hallmark of desiccation tolerance in the resurrection species is the accumulation of protective late embryogenesis abundant proteins (LEAPs). These intrinsically disordered proteins (IDPs) may stabilize the correct structure of proteins and membranes during cellular dehydration. The aim of our study was to assess LEA genes’ expression levels in hydrated (HL) and desiccated leaves (DL) and to identify, characterise, and estimate the potential role of R. serbica LEAPs in desiccation tolerance. In total, 318 LEAPs from HL and DL were identified and classified into the seven LEA protein family groups ranging from LEA1-LEA5, seed maturation proteins (SMPs), and dehydrins (DEH). Analysis of the physicochemical properties, motif architecture, secondary structure, homology, and phylogenetic relationships demonstrated that R. serbica LEAPs greatly differed among the LEA family groups. The most abundant LEA2 proteins (mostly downregulated upon desiccation) exhibited lower hydrophilicity and propensity to fold into organised globular domains. Oppositely, hydrophilic LEA4 proteins tended to form amphipathic, A-type, α-helices. Most of desiccation-upregulated LEA genes encoded highly disordered DEH1, LEA1, LEA4.2, and LEA4.3 proteins. While dehydrins might chelate metals and bind DNA under water deficit, other ID LEAPs (e.g. LEA1, LEA3, LEA4) might participate in forming intracellular proteinaceous condensates or adopt amphipathic α-helical conformation, enabling them to stabilise desiccation-sensitive proteins and membranes. Taken together, possible functions of LEAPs are discussed with significant implications on drought tolerance improvement of crops grown in arid areas. PB - Serbian Plant Physiology Society PB - Institute for Biological Research “Siniša Stanković” – National Institute of Republic of Serbia, University of Belgrade PB - Faculty of Biology, University of Belgrade C3 - Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83- T1 - Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization SP - 95 UR - https://hdl.handle.net/21.15107/rcub_rimsi_3085 ER -
@conference{ author = "Pantelic, Ana and Stevanovic, Strahinja and Milić, Dejana and Milić Komić, Sonja and Kilibarda, Nataša and Vidović, Marija", year = "2022", abstract = "An ancient resurrection plant Ramonda serbica Panc. is able to survive a long desiccation period and reestablish metabolic activity upon watering. A hallmark of desiccation tolerance in the resurrection species is the accumulation of protective late embryogenesis abundant proteins (LEAPs). These intrinsically disordered proteins (IDPs) may stabilize the correct structure of proteins and membranes during cellular dehydration. The aim of our study was to assess LEA genes’ expression levels in hydrated (HL) and desiccated leaves (DL) and to identify, characterise, and estimate the potential role of R. serbica LEAPs in desiccation tolerance. In total, 318 LEAPs from HL and DL were identified and classified into the seven LEA protein family groups ranging from LEA1-LEA5, seed maturation proteins (SMPs), and dehydrins (DEH). Analysis of the physicochemical properties, motif architecture, secondary structure, homology, and phylogenetic relationships demonstrated that R. serbica LEAPs greatly differed among the LEA family groups. The most abundant LEA2 proteins (mostly downregulated upon desiccation) exhibited lower hydrophilicity and propensity to fold into organised globular domains. Oppositely, hydrophilic LEA4 proteins tended to form amphipathic, A-type, α-helices. Most of desiccation-upregulated LEA genes encoded highly disordered DEH1, LEA1, LEA4.2, and LEA4.3 proteins. While dehydrins might chelate metals and bind DNA under water deficit, other ID LEAPs (e.g. LEA1, LEA3, LEA4) might participate in forming intracellular proteinaceous condensates or adopt amphipathic α-helical conformation, enabling them to stabilise desiccation-sensitive proteins and membranes. Taken together, possible functions of LEAPs are discussed with significant implications on drought tolerance improvement of crops grown in arid areas.", publisher = "Serbian Plant Physiology Society, Institute for Biological Research “Siniša Stanković” – National Institute of Republic of Serbia, University of Belgrade, Faculty of Biology, University of Belgrade", journal = "Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83-", title = "Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization", pages = "95", url = "https://hdl.handle.net/21.15107/rcub_rimsi_3085" }
Pantelic, A., Stevanovic, S., Milić, D., Milić Komić, S., Kilibarda, N.,& Vidović, M.. (2022). Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization. in Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83- Serbian Plant Physiology Society., 95. https://hdl.handle.net/21.15107/rcub_rimsi_3085
Pantelic A, Stevanovic S, Milić D, Milić Komić S, Kilibarda N, Vidović M. Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization. in Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83-. 2022;:95. https://hdl.handle.net/21.15107/rcub_rimsi_3085 .
Pantelic, Ana, Stevanovic, Strahinja, Milić, Dejana, Milić Komić, Sonja, Kilibarda, Nataša, Vidović, Marija, "Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization" in Book of Abstracts / 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade, 2022, 83- (2022):95, https://hdl.handle.net/21.15107/rcub_rimsi_3085 .