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

Nikoletta Murvai, Lajos Kalmar, Bianka Szalaine Agoston, Beata Szabo, Agnes Tantos, Gyorgy Csikos, András Micsonai, József Kardos, Didier Vertommen, Phuong N. Nguyen, Nevena Hristozova, Andras Lang, Denes Kovacs, Laszlo Buday, Kyou Hoon Han, Andras Perczel, Peter Tompa

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
JournalCells
Volume9
Issue number8
DOIs
Publication statusPublished - Aug 7 2020

Keywords

  • cell protection
  • chaperone
  • client protein
  • in-cell NMR
  • intrinsic structural disorder
  • pre-structured motif

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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. (2020). Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14. Cells, 9(8). https://doi.org/10.3390/cells9081856