The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.

@article{Denoncin2010ThePI,
  title={The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.},
  author={Katleen Denoncin and Didier Vertommen and Eunok Paek and Jean-Francois Collet},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 38},
  pages={29425-33}
}
The assembly of the β-barrel proteins present in the outer membrane (OM) of Gram-negative bacteria is poorly characterized. After translocation across the inner membrane, unfolded β-barrel proteins are escorted across the periplasm by chaperones that reside within this compartment. Two partially redundant chaperones, SurA and Skp, are considered to transport the bulk mass of β-barrel proteins. We found that the periplasmic disulfide isomerase DsbC cooperates with SurA and the thiol oxidase DsbA… CONTINUE READING
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