Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress.

NMR spectroscopy atomic force microscopy gels intrinsically disordered proteins tardigrades

Journal

Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543

Informations de publication

Date de publication:
03 01 2022
Historique:
revised: 03 11 2021
received: 26 07 2021
pubmed: 10 11 2021
medline: 18 1 2022
entrez: 9 11 2021
Statut: ppublish

Résumé

Tardigrades are remarkable for their ability to survive harsh stress conditions as diverse as extreme temperature and desiccation. The molecular mechanisms that confer this unusual resistance to physical stress remain unknown. Recently, tardigrade-unique intrinsically disordered proteins have been shown to play an essential role in tardigrade anhydrobiosis. Here, we characterize the conformational and physical behaviour of CAHS-8 from Hypsibius exemplaris. NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini. Upon concentration, the protein is shown to successively form oligomers, long fibres, and finally gels constituted of fibres in a strongly temperature-dependent manner. The helical domain forms the core of the fibrillar structure, with the disordered termini remaining highly dynamic within the gel. Soluble proteins can be encapsulated within cavities in the gel, maintaining their functional form. The ability to reversibly form fibrous gels may be associated with the enhanced protective properties of these proteins.

Identifiants

pubmed: 34750927
doi: 10.1002/anie.202109961
pmc: PMC9299615
doi:

Substances chimiques

Gels 0
Intrinsically Disordered Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e202109961

Subventions

Organisme : anr
ID : ANR-10-INBS-05-02
Organisme : anr
ID : ANR-17-EURE-0003
Organisme : ERC
ID : DynamicAssemblies

Informations de copyright

© 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.

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Auteurs

Anas Malki (A)

Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.

Jean-Marie Teulon (JM)

Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.

Aldo R Camacho-Zarco (AR)

Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.

Shu-Wen W Chen (SW)

niChe Lab for Stem Cell and Regenerative Medicine, Department of Biochemical Science and Technology, National (Taiwan) University, Taipei, 10617, Taiwan.

Wiktor Adamski (W)

Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.

Damien Maurin (D)

Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.

Nicola Salvi (N)

Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.

Jean-Luc Pellequer (JL)

Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.

Martin Blackledge (M)

Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.

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