Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.

@article{Bader2001TurningAD,
  title={Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.},
  author={Martin W Bader and Annie Hiniker and James Regeimbal and David C Goldstone and Peter Haebel and Jan Riemer and P. Metcalf and James C. A. Bardwell},
  journal={The EMBO journal},
  year={2001},
  volume={20 7},
  pages={
          1555-62
        }
}
There are two distinct pathways for disulfide formation in prokaryotes. The DsbA-DsbB pathway introduces disulfide bonds de novo, while the DsbC-DsbD pathway functions to isomerize disulfides. One of the key questions in disulfide biology is how the isomerase pathway is kept separate from the oxidase pathway in vivo. Cross-talk between these two systems would be mutually destructive. To force communication between these two systems we have selected dsbC mutants that complement a dsbA null… CONTINUE READING

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