Coevolution in human small Heat Shock Protein 1 is promoted by interactions between the Alpha-Crystallin domain and the disordered regions.

ABSTRACT: Human small Heat Shock Protein 1 (HSPB1) belongs to the Small Heat Shock Protein (sHSP) superfamily, a group of ATP-independent molecular chaperones essential for cellular stress responses and protein quality control. These proteins share a conserved domain organization, with a structured Alpha-Crystallin domain (ACD) flanked by disordered N-terminal and C-terminal regions (NTR and CTR). While the prevailing evolutionary hypothesis for the sHSP family suggests that the disordered regions evolved independently and at a faster rate than the ACD, this study provides, for the first time, evidence of coevolution between these regions in human HSPB1, introducing new insights into the evolutionary mechanisms that sustain critical regulatory interactions. By integrating evolutionary and structural

SUBMITTER: Racigh V 

PROVIDER: S-EPMC12052118 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature