Engineered pathways for correct disulfide bond oxidation.

@article{Ren2011EngineeredPF,
  title={Engineered pathways for correct disulfide bond oxidation.},
  author={Guoping Ren and James C. A. Bardwell},
  journal={Antioxidants & redox signaling},
  year={2011},
  volume={14 12},
  pages={2399-412}
}
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking protein disulfide isomerases (PDIs) can use alternative mechanisms for correct disulfide bond formation. By linking correct disulfide bond formation to antibiotic resistance, we selected mutants that catalyze correct disulfide formation in the absence of DsbC, Escherichia coli's PDI. Most of our mutants massively overproduce the disulfide oxidase DsbA and change its redox status. They enhance DsbA's… CONTINUE READING