Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.

@article{Bertoli2004TwoCC,
  title={Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.},
  author={Gloria Bertoli and Thomas Simmen and Tiziana Anelli and Silvia Nerini Molteni and R. Fesce and Roberto Sitia},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 29},
  pages={30047-52}
}
Human Ero1alpha is an endoplasmic reticulum (ER)-resident protein responsible for protein disulfide isomerase (PDI) oxidation. To clarify the molecular mechanisms underlying its function, we generated a panel of cysteine replacement mutants and analyzed their capability of: 1) complementing a temperature-sensitive yeast Ero1 mutant, 2) favoring oxidative folding in mammalian cells, 3) forming mixed disulfides with PDI and ERp44, and 4) adopting characteristic redox-dependent conformations. Our… CONTINUE READING

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