Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14
Open accessAbstract
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.
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The Arabidopsis thaliana dehydrin ERD14 can increase the viability of E. coli subjected to 15 min at 50 °C.
“The Arabidopsis thaliana dehydrin Early Response to Dehydration 14 (ERD14) can increase the viability of E. coli subjected to 15 min at 50 °C [230].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [230]
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- Authors
- 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.
- Affiliations
- Institute of Molecular Life Sciences (HU)
- Institute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary
- Department of General Zoology, Eötvös Loránd University, 1117 Budapest, Hungary
- Eötvös Loránd University (HU)
- de Duve Institute (BE)
- Vrije Universiteit Brussel (BE)
- MTA-ELTE Protein Modelling Research Group and Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös L. University, 1117 Budapest, Hungary
- Structural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium
- Korea Research Institute of Bioscience and Biotechnology (KR)
- ORCID
- Venue
- Cells
- Publisher
- MDPI AG
- Published
- 2020-08-07
- Volume
- 9
- Issue
- 8
- Pages
- 1856
- ISSN
- 2073-4409 (ISSN-L)
- PMC
- PMC7465474
- OpenAlex
- W3048198009
- Cited by
- 13
- References
- 79
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 2 · 2022: 3 · 2021: 4
- FWCI
- 0.73
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cells (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Repository of the Academy's Library (Library of the Hungarian Academy of Sciences) (acceptedVersion)
- Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- VUBIR (Vrije Universiteit Brussel) (submittedVersion)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- Apollo (cc-by)
- Funders
- Fonds Wetenschappelijk Onderzoek (G.0029.12)
- Hungarian Scientific Research Fund (K124670, K131702, K125340)
- National Research Council of Science and Technology (NTM2231712)
- Korea-Hungarian Joint Laboratory program (2010-88343)
- Magyar Tudományos Akadémia (Lendulet)
- Hungarian Ministry of Human Capacities (VEKOP-2.3.3-15-2016-00009, VEKOP-2.3.2-16-2017-00014)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- dehydrins, intrinsically disordered proteins, chaperone activity, in-cell NMR, K-segment, S segment, Arabidopsis thaliana, Escherichia coli
- MeSH terms
- Protein Domains, Microorganisms, Genetically-Modified, Escherichia coli, Protein Binding, Arabidopsis, Molecular Chaperones, Heat-Shock Response, Proteome, Arabidopsis Proteins, Microbial Viability, Intrinsically Disordered Proteins
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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