The Ribosome Cooperates with a Chaperone to Guide Multi-domain Protein Folding.

ABSTRACT: Multi-domain proteins, containing several structural units within a single polypeptide, constitute a large fraction of all proteomes. Co-translational folding is assumed to simplify the conformational search problem for large proteins, but the events leading to correctly folded, functional structures remain poorly characterized. Similarly, how the ribosome and molecular chaperones promote efficient folding remains obscure. Using optical tweezers, we have dissected early folding events of nascent elongation factor G, a multi-domain protein that requires chaperones for folding. The ribosome and the chaperone trigger factor reduce inter-domain misfolding, permitting folding of the N-terminal G-domain. Successful completion of this step is a crucial prerequisite for folding of the next domain.

SUBMITTER: Liu K 

PROVIDER: S-EPMC6481645 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature