A pathway for disulfide bond formation in vivo

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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.
Publisher
National Academy of Sciences
Issue Date
1993
Language
English
Citation

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.90, no.3, pp.1038 - 1042

ISSN
0027-8424
URI
http://hdl.handle.net/10203/65249
Appears in Collection
CH-Journal Papers(저널논문)
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