مؤتمر
Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization
| العنوان: | Late embryogenesis abundant (LEA) proteins in Ramonda serbica Panc identification, classification and structural characterization |
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| المؤلفون: | Pantelić, Ana, Stevanović, Strahinja, Milić, Dejana, Milić Komić, Sonja, Kilibarda, Nataša, Vidović, Marija |
| المساهمون: | Milutinović, Milica |
| المصدر: | 4th International Conference on Plant Biology and 23rd SPPS Meeting |
| بيانات النشر: | 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 |
| سنة النشر: | 2022 |
| مصطلحات موضوعية: | 3D protein structure modelling, de novo transcriptome assembly, intrinsically disordered proteins, liquid-liquid phase separation, secondary structure prediction |
| الوصف: | 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. ; Book of Abstracts: 4th International Conference on Plant Biology [and] 23rd SPPS Meeting, 6-8 October 2022, Belgrade |
| نوع الوثيقة: | conference object |
| اللغة: | English |
| ردمك: | 978-86-912591-6-7 86-912591-6-7 |
| العلاقة: | This research was funded by the Science Fund of the Republic of Serbia-RS (PROMIS project LEAPSyn-SCI, grant no. 6039663); info:eu-repo/grantAgreement/MESTD/inst-2020/200042/RS//; https://imagine.imgge.bg.ac.rs/handle/123456789/1846Test; https://imagine.imgge.bg.ac.rs/bitstream/id/194912/Late_embry_genesis_abundant_LEA_proteins_in_Ramonda_serbica_Panc_identification_classification_and_structural_characterization_2022.pdfTest; https://hdl.handle.net/21.15107/rcub_imagine_1846Test |
| الإتاحة: | https://imagine.imgge.bg.ac.rs/handle/123456789/1846Test https://imagine.imgge.bg.ac.rs/bitstream/id/194912/Late_embry_genesis_abundant_LEA_proteins_in_Ramonda_serbica_Panc_identification_classification_and_structural_characterization_2022.pdfTest https://hdl.handle.net/21.15107/rcub_imagine_1846Test |
| حقوق: | openAccess ; ARR |
| رقم الانضمام: | edsbas.146650EA |
| قاعدة البيانات: | BASE |
| ردمك: | 9788691259167 8691259167 |
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