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

Autor: Malki A; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France., Teulon JM; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France., Camacho-Zarco AR; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France., Chen SW; niChe Lab for Stem Cell and Regenerative Medicine, Department of Biochemical Science and Technology, National (Taiwan) University, Taipei, 10617, Taiwan., Adamski W; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France., Maurin D; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France., Salvi N; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France., Pellequer JL; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France., Blackledge M; Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Grenoble, France.
Jazyk: angličtina
Zdroj: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2022 Jan 03; Vol. 61 (1), pp. e202109961. Date of Electronic Publication: 2021 Nov 25.
DOI: 10.1002/anie.202109961
Abstrakt: 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.
(© 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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