查看文章

Small heat shock proteins (sHsps) are one of the most ubiquitous molecular chaperones. They are grouped together based on a conserved domain, the α‐crystallin domain. Generally, sHsps exist as oligomers of 9–40 subunits, and the oligomers undergo reversible temperature‐dependent dissociation into smaller species as dimers, which interact with denaturing substrate proteins. Previous studies have shown that the C‐terminal region, especially the consensus IXI/V motif, is responsible for oligomer assembly. In this study, we examined deletions or mutations in the C‐terminal region on the oligomer assembly and function of StHsp14.0, an sHsp from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7. Mutated StHsp14.0 with C‐terminal deletion or replacement of IIe residues in the IXI/V motif to Ala, Ser, or Phe residues could not form large oligomers and lost chaperone activity. StHsp14.0WKW, whose …