Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.

ABSTRACT: Polypeptide chains experience mechanical tension while translocating through cellular tunnels, which are subsequently folded by molecular chaperones. However, interactions between tunnel-associated chaperones and these emerging polypeptides under force is not completely understood. Our investigation focused on mechanical chaperone activity of two tunnel-associated chaperones, BiP and ERdj3 both with and without mechanical constraints and comparing them with their cytoplasmic homologs: DnaK and DnaJ. While BiP/ERdj3 have been observed to exhibit robust foldase activity under force, DnaK/DnaJ showed holdase function. Importantly, the tunnel-associated chaperones (BiP/ERdj3) transitioned to a holdase state in the absence of force, indicating a force-dependent chaperone behavior. This chaperon

SUBMITTER: Banerjee S 

PROVIDER: S-EPMC11168073 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature