Hsp90, DnaK, and ClpB collaborate in protein reactivation.

ABSTRACT: Hsp70, Hsp90, and ClpB/Hsp100 are molecular chaperones that help regulate proteostasis. Bacterial and yeast Hsp70s and their cochaperones function synergistically with Hsp90s to reactivate inactive and aggregated proteins by a mechanism that requires a direct interaction between Hsp90 and Hsp70 both in vitro and in vivo. Escherichia coli and yeast Hsp70s also collaborate in bichaperone systems with ClpB and Hsp104, respectively, to disaggregate and reactivate aggregated proteins and amyloids such as prions. These collaborations are dependent on direct interactions between ClpB/Hsp104 and Hsp70. We explored the possibility that E. coli homologs of Hsp70, Hsp90, and ClpB, referred to as DnaK, Hsp90_Ec, and ClpB, respectively, in combination with two DnaK cochaperones,

SUBMITTER: Hoskins JR 

PROVIDER: S-EPMC11804706 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature