ArticleProtein science : a publication of the Protein Society2024
Helicity of a tardigrade disordered protein contributes to its protective function during desiccation.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Cytoplasmic abundant heat-soluble proteins from tardigrades protect synthetic cells under stress.Nature communications · 2026Article
- Surviving desiccation: key factors underlying tolerance in prokaryotes and eukaryotes.Protoplasma · 2025Review
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- Life on the dry side: a roadmap to understanding desiccation tolerance and accelerating translational applications.Nature communications · 2025Review
- Diversity in the protective role(s) of the conserved motif 1 from tardigrade cytoplasmic-abundant heat-soluble proteins during drying.Protein science : a publication of the Protein Society · 2025Article
- An evaluation of thermal tolerance in six tardigrade species in an active and dry state.Biology open · 2024Article
- Structural adaptability and surface activity of peptides derived from tardigrade proteins.Protein science : a publication of the Protein Society · 2024Article
- Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024Article
- Helicity of a tardigrade disordered protein contributes to its protective function during desiccation.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
To survive extreme drying (anhydrobiosis), many organisms, spanning every kingdom of life, accumulate intrinsically disordered proteins (IDPs). For decades, the ability of anhydrobiosis-related IDPs to form transient amphipathic helices has been suggested to be important for promoting desiccation tolerance. However, evidence empirically supporting the necessity and/or sufficiency of helicity in mediating anhydrobiosis is lacking. Here, we demonstrate that the linker region of CAHS D, a desiccation-related IDP from the tardigrade Hypsibius exemplaris, that contains significant helical structure, is the protective portion of this protein. Perturbing the sequence composition and grammar of the linker region of CAHS D, through the insertion of helix-breaking prolines, modulating the identity of charged residues, or replacement of hydrophobic amino acids with serine or glycine residues results in variants with different degrees of helical structure. Importantly, correlation of protective capacity and helical content in variants generated through different helix perturbing modalities does not show as strong a trend, suggesting that while helicity is important, it is not the only property that makes a protein protective during desiccation. These results provide direct evidence for the decades-old theory that helicity of desiccation-related IDPs is linked to their anhydrobiotic capacity.
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