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Proc Natl Acad Sci U S A. 1993 Feb 1;90(3):1038-42.

A pathway for disulfide bond formation in vivo.

Author information

1
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.

Abstract

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.

PMID:
8430071
PMCID:
PMC45806
[Indexed for MEDLINE]
Free PMC Article
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