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A pathway for disulfide bond formation in vivo.


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.

SUBMITTER: Bardwell JC 

PROVIDER: S-EPMC45806 | biostudies-other | 1993 Feb

REPOSITORIES: biostudies-other

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A pathway for disulfide bond formation in vivo.

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]

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