Two novel heat-soluble protein families abundantly expressed in an anhydrobiotic tardigrade
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SAHS1 identified as major heat-soluble protein by proteomics
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SAHS1 is a secretory protein confirmed by GFP fusion experiments
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Undergoes conformational change to alpha-helix in water-deficient conditions
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Proposed to act as molecular shield protecting extracellular components during desiccation
Extremotolerant tardigrade genome and improved radiotolerance of human cultured cells by tardigrade-unique protein
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Genome sequencing confirmed 13 SAHS genes in R. varieornatus
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SAHS genes are constitutively and abundantly expressed
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SAHS proteins have low similarity to metazoan fatty acid-binding proteins
Structural insights into a secretory abundant heat-soluble protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus
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Crystal structure of SAHS1 solved at 1.45 angstrom resolution (PDB 5XN9)
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Beta-barrel fold similar to FABPs but with unique hydrophilic hydrogen bond networks
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Two putative ligand-binding sites identified
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SAHS proteins constitute a new FABP family adapted for desiccation tolerance
Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt