PMID:8430071

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Citation

Bardwell, JC, Lee, JO, Jander, G, Martin, N, Belin, D and Beckwith, J (1993) A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. U.S.A. 90:1038-42

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.

Links

PubMed PMC45806

Keywords

Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cysteine/metabolism; Cystine/metabolism; Disulfides/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Genes, Bacterial; Isomerases/genetics; Isomerases/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Models, Biological; Molecular Sequence Data; Mutagenesis; Oxidoreductases/genetics; Oxidoreductases/metabolism; Protein Disulfide-Isomerases; Protein Processing, Post-Translational

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