Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ.

@article{Mattison2002PhosphorylationAT,
  title={Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ.},
  author={Kirsten Mattison and Linda J Kenney},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 13},
  pages={11143-8}
}
OmpR and EnvZ comprise a two-component system that regulates the porin genes ompF and ompC in response to changes in osmolarity. EnvZ is autophosphorylated by intracellular ATP on a histidine residue, and it transfers the phosphoryl group to an aspartic acid residue of OmpR. EnvZ can also dephosphorylate phospho-OmpR (OmpR-P) to control the cellular level of OmpR-P. At low osmolarity, OmpR-P levels are low because of either low EnvZ kinase or high EnvZ phosphatase activities. At high osmolarity… CONTINUE READING

From This Paper

Topics from this paper.
25 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 25 extracted citations

Similar Papers

Loading similar papers…