A pathway for disulfide bond formation in vivo.
1993; National Academy of Sciences; Volume: 90; Issue: 3 Linguagem: Inglês
10.1073/pnas.90.3.1038
ISSN1091-6490
AutoresJames C.A. Bardwell, Jie‐Oh Lee, Georg Jander, Nancy Martin, Dominique Belin, J Beckwith,
Tópico(s)ATP Synthase and ATPases Research
ResumoProtein 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.
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