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Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14

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Murvai, Nikoletta 
Kalmar, Lajos 
Szabo, Beata 
Schad, Eva 
Micsonai, András 


Disordered plant chaperones play key roles in helping plants survive in harsh conditions, and they are indispensable for seeds to remain viable. Aside from well-known and thoroughly characterized globular chaperone proteins, there are a number of intrinsically disordered proteins (IDPs) that can also serve as highly effective protecting agents in the cells. One of the largest groups of disordered chaperones is the group of dehydrins, proteins that are expressed at high levels under different abiotic stress conditions, such as drought, high temperature, or osmotic stress. Dehydrins are characterized by the presence of different conserved sequence motifs that also serve as the basis for their categorization. Despite their accepted importance, the exact role and relevance of the conserved regions have not yet been formally addressed. Here, we explored the involvement of each conserved segment in the protective function of the intrinsically disordered stress protein (IDSP) A. thaliana’s Early Response to Dehydration (ERD14). We show that segments that are directly involved in partner binding, and others that are not, are equally necessary for proper function and that cellular protection emerges from the balanced interplay of different regions of ERD14.



intrinsic structural disorder, plant chaperone, heat stress, structure-function relationship, dehydrin, early response to dehydration, LEA protein, CD spectroscopy

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International Journal of Molecular Sciences

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Research Foundation Flanders (G.0029.12)
Korea Research Council of Fundamental Science and Technology (2010-88343)
National Research Council of Science and Technology (NTM2231712)
National Research, Development and Innovation Office, Hungary (K124670, K131702, K125340, K120391, KH125597, PD135510, 20171582, 20180805, 20181890)
Hungarian Academy of Sciences (Bolyai János Scholarship, Lendület Grant)