Ontology highlight
ABSTRACT:
SUBMITTER: Bardwell JC
PROVIDER: S-EPMC45806 | biostudies-other | 1993 Feb
REPOSITORIES: biostudies-other
Bardwell J C JC Lee J O JO Jander G G Martin N N Belin D D Beckwith J J
Proceedings of the National Academy of Sciences of the United States of America 19930201 3
Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations in the gene for a second protein, DsbB, which is also necessary for disulfide bond formation. Evidence suggests that DsbB may act by reoxidizing DsbA, thereby regenerating its ability to donate its disulfide bond to target proteins. We propose that DsbB, an integral membrane protein, may be involved in transducing redox potential across the cytoplasmic membrane. ...[more]