The ribosome destabilizes native and non-native structures in a nascent multidomain protein.

ABSTRACT: Correct folding is a prerequisite for the biological activity of most proteins. Folding has largely been studied using in vitro refolding assays with isolated small, robustly folding proteins. A substantial fraction of all cellular proteomes is composed of multidomain proteins that are often not amenable to this approach, and their folding remains poorly understood. These large proteins likely begin to fold during their synthesis by the ribosome, a large molecular machine that translates the genetic code. The ribosome affects how folding proceeds, but the underlying mechanisms remain largely obscure. We have utilized optical tweezers to study the folding of elongation factor G, a multidomain protein composed of five domains. We find that interactions among unfolded domains interfere with p

SUBMITTER: Liu K 

PROVIDER: S-EPMC5477528 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature