@article{90046,
  keywords = {phosphorylation, signal transduction, Escherichia coli, Mutagenesis, Gene Expression Regulation, Bacterial, Repressor Proteins, Models, Biological, Phosphoproteins, Recombinant Fusion Proteins, Genetic Complementation Test, Genes, Regulator, beta-Galactosidase, Diploidy, Plasmids, Bacterial Outer Membrane Proteins, Phosphoprotein Phosphatases, Porins, Water-Electrolyte Balance, Bacteriophages},
  author = {Russo and Silhavy},
  title = {EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes},
  abstract = {<p>Osmoregulation of the bacterial porin genes ompF and ompC is controlled by a two-component regulatory system. EnvZ, the sensor component of this system, is capable both of phosphorylating and dephosphorylating OmpR, the effector component. Mutations were isolated in envZ that abolish the expression of both porin genes. These mutants appear to have lost the kinase activity of EnvZ while retaining their phosphatase activity, so that in their presence OmpR is completely unphosphorylated. The behavior of these mutants in haploid, and in diploid with other envZ alleles, is consistent with a model in which EnvZ mediates osmoregulation by controlling the concentration of a single species. OmpR-P.</p>
},
  year = {1991},
  journal = {J Mol Biol},
  volume = {222},
  pages = {567-80},
  month = {12/1991},
  issn = {0022-2836},
  doi = {10.1016/0022-2836(91)90497-t},
  language = {eng},
}