Cysteine-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase.

@article{Qin2003CysteinescanningAO,
  title={Cysteine-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase.},
  author={Ling Qin and Shengjian Cai and Yan Zhu and M. Inouye},
  journal={Journal of bacteriology},
  year={2003},
  volume={185 11},
  pages={3429-35}
}
EnvZ and OmpR are a transmembrane sensor and its cognate response regulator, respectively, regulating the transcription of porin genes in response to medium osmolarity in Escherichia coli. The cytoplasmic domain of EnvZ (EnvZc) possesses both kinase and phosphatase activities and can be dissected into two functional domains, A and B. Here, we performed a cysteine-scanning analysis of domain A, a 67-residue central dimerization and phosphatase domain containing His-243 as the phosphorylation… CONTINUE READING

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