Quantitative Analyses of the Yeast Oxidative Protein Folding Pathway In Vitro and In Vivo.

ABSTRACT: Aims: Efficient oxidative protein folding (OPF) in the endoplasmic reticulum (ER) is a key requirement of the eukaryotic secretory pathway. In particular, protein folding linked to the formation of disulfide bonds, an activity dependent on the enzyme protein disulfide isomerase (PDI), is crucial. For the de novo formation of disulfide bonds, reduced PDI must be reoxidized by an ER-located oxidase (ERO1). Despite some knowledge of this pathway, the kinetic parameters with which these components act and the importance of specific parameters, such as PDI reoxidation by Ero1, for the overall performance of OPF in vivo remain poorly understood. Results: We established an in vitro system using purified yeast (Saccharomyces cerevisiae) PDI (

SUBMITTER: Beal DM 

PROVIDER: S-EPMC6602113 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature