Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation.

ABSTRACT: The relationship between protein synthesis, folding, and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested that pre-existing disulfide links are absolutely required to allow protein folding and, conversely, that protein folding occurs prior to disulfide formation. To address the question of what happens first within the ER, that is, protein folding or disulfide formation, we studied folding events at the early stages of polypeptide chain translocation into the mammalian ER using stalled translation intermediates. Our results demonstrate that polypeptide folding can occur without complete domain translocation. Protein disulfide isomerase (PDI) interacts with these early intermediates, but disulfide formation does not occur unless

SUBMITTER: Robinson PJ 

PROVIDER: S-EPMC5409466 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature