Prefoldin, a jellyfish-like molecular chaperone: functional cooperation with a group II chaperonin and beyond.

ABSTRACT: Prefoldin is a hexameric molecular chaperone found in the cytosol of archaea and eukaryotes. Its hexameric complex is built from two related classes of subunits and has the appearance of a jellyfish: its body consists of a double beta-barrel assembly with six long tentacle-like coiled coils protruding from it. Using the tentacles, prefoldin captures an unfolded protein substrate and transfers it to a group II chaperonin. The prefoldin-group II chaperonin system is thought to be important for the folding of newly synthesized proteins and for their maintenance, or proteostasis, in the cytosol. Based on structural information of archaeal prefoldins, the mechanisms of substrate recognition and prefoldin-chaperonin cooperation have been investigated. In contrast, the role and mechanism of eukar

SUBMITTER: Sahlan M 

PROVIDER: S-EPMC5899742 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature