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Open AccessArticle

Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14

1
Institute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary
2
Department of Veterinary Medicine, University of Cambridge, Cambridge CB3 0ES, UK
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MTA-ELTE Protein Modelling Research Group and Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös L. University, 1117 Budapest, Hungary
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Department of General Zoology, Eötvös Loránd University, 1117 Budapest, Hungary
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ELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, Eötvös Loránd University, 1117 Budapest, Hungary
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Faculty of Medicine and de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium
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Structural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium
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VIB-VUB Center for Structural Biology (CSB), Vlaams Instituut voor Biotechnologie (VIB), 1050 Brussels, Belgium
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Gene Editing Research Center, Division of Convergent Biomedical Research, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea
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Biomedical Translational Research Center, Division of Convergent Biomedical Research, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea
*
Author to whom correspondence should be addressed.
Cells 2020, 9(8), 1856; https://doi.org/10.3390/cells9081856
Received: 16 June 2020 / Revised: 16 July 2020 / Accepted: 30 July 2020 / Published: 7 August 2020
(This article belongs to the Section Plant, Algae and Fungi Cell Biology)
Details of the functional mechanisms of intrinsically disordered proteins (IDPs) in living cells is an area not frequently investigated. Here, we dissect the molecular mechanism of action of an IDP in cells by detailed structural analyses based on an in-cell nuclear magnetic resonance experiment. We show that the ID stress protein (IDSP) A. thaliana Early Response to Dehydration (ERD14) is capable of protecting E. coli cells under heat stress. The overexpression of ERD14 increases the viability of E. coli cells from 38.9% to 73.9% following heat stress (50 °C × 15 min). We also provide evidence that the protection is mainly achieved by protecting the proteome of the cells. In-cell NMR experiments performed in E. coli cells show that the protective activity is associated with a largely disordered structural state with conserved, short sequence motifs (K- and H-segments), which transiently sample helical conformations in vitro and engage in partner binding in vivo. Other regions of the protein, such as its S segment and its regions linking and flanking the binding motifs, remain unbound and disordered in the cell. Our data suggest that the cellular function of ERD14 is compatible with its residual structural disorder in vivo. View Full-Text
Keywords: intrinsic structural disorder; chaperone; in-cell NMR; pre-structured motif; client protein; cell protection intrinsic structural disorder; chaperone; in-cell NMR; pre-structured motif; client protein; cell protection
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Murvai, N.; Kalmar, L.; Szalaine Agoston, B.; Szabo, B.; Tantos, A.; Csikos, G.; Micsonai, A.; Kardos, J.; Vertommen, D.; Nguyen, P.N.; Hristozova, N.; Lang, A.; Kovacs, D.; Buday, L.; Han, K.-H.; Perczel, A.; Tompa, P. Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14. Cells 2020, 9, 1856.

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