Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 61, Issue 1, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202109961
Keywords
atomic force microscopy; gels; intrinsically disordered proteins; NMR spectroscopy; tardigrades
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Funding
- FRISBI [ANR-10-INBS-05-02]
- GRAL within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS [ANR-17-EURE-0003]
- ERC advanced grant DynamicAssemblies
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The study characterizes the conformational and physical behavior of CAHS-8 protein from Hypsibius exemplaris, showing its ability to form fibrous gels that may enhance the protective properties of the proteins. This unique ability of reversible formation of fibrous gels could be associated with the exceptional resistance of tardigrades to harsh stress conditions.
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.
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