Hsp110 nucleotide exchange factors may amplify Hsp70-disaggregation by enhanced entropic pulling.

ABSTRACT: Hsp70s use energy from ATP hydrolysis to unfold protein structures and solubilize stable aggregates and accumulate native species, even under adverse non-native conditions. To carry out its catalytic polypeptide-unfolding activity, Hsp70 needs to reversibly interact with a J-domain (JDP) catalyst, a misfolded or alternatively-folded polypeptide substrate and a nucleotide exchange factor (NEF), which binds to the nucleotide-binding domain (NBD), accelerates ADP-release, and controls the dissociation of the unfolded polypeptide product of the unfolding reaction. In bacteria, GrpE is the ubiquitous NEF, and yet, during the process of eukaryotization, it was lost from the cytosol, to be replaced by novel NEF proteins, among which the Hsp110 family stands out. Curiously, Hsp110s belong to the H

SUBMITTER: Rebeaud ME 

PROVIDER: S-EPMC12305717 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature