Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.

ABSTRACT: As newly synthesized polypeptides emerge from the ribosome, it is crucial that they fold correctly. To prevent premature aggregation, nascent chains interact with chaperones that facilitate folding or prevent misfolding until protein synthesis is complete. Nascent polypeptide-associated complex (NAC) is a ribosome-associated chaperone that is important for protein homeostasis. However, how NAC binds its substrates remains unclear. Using native electrospray ionization MS (ESI-MS), limited proteolysis, NMR, and cross-linking, we analyzed the conformational properties of NAC from Caenorhabditis elegans and studied its ability to bind proteins in different conformational states. Our results revealed that NAC adopts an array of compact and expanded conformations and binds weakly to clien

SUBMITTER: Martin EM 

PROVIDER: S-EPMC5986199 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature