Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch.

@article{Paget2001MutationalAO,
  title={Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch.},
  author={Mark S. B. Paget and J. B. Bae and M Y Hahn and Wenhui Li and Colin Kleanthous and Jung Hye Roe and Mark J. Buttner},
  journal={Molecular microbiology},
  year={2001},
  volume={39 4},
  pages={1036-47}
}
In the Gram-positive bacterium, Streptomyces coelicolor A3(2), expression of the thioredoxin system is modulated by a sigma factor called sigmaR in response to changes in the cytoplasmic thiol-disulphide status, and the activity of sigmaR is controlled post-translationally by an anti-sigma factor, RsrA. In vitro, the anti-sigma factor activity of RsrA, which contains seven cysteines, correlates with its thiol-disulphide redox status. Here, we investigate the function of RsrA in vivo. A… CONTINUE READING

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