GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome.

ABSTRACT: The bacterial chaperonin GroEL/ES promotes protein folding post-translation by transiently encapsulating client proteins within a central chamber. GroEL also binds translating ribosomes in vivo, implying an additional role in cotranslational folding. However, how GroEL/ES recognises and modulates ribosome-tethered nascent proteins is unclear. Here, we used biochemical reconstitution, structural proteomics and electron microscopy to study the mechanism by which GroEL/ES engages nascent polypeptides. We show that GroEL binds nascent chains on the inside of its cavity via the apical domains and disordered C-terminal tails, resulting in local structural destabilization of the client. Ribosome-tethered nascent domains are partially encapsulated upon GroES binding to GroEL, and recover their ori

SUBMITTER: Roeselova A 

PROVIDER: S-EPMC12615815 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature