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Papers In Press, published online ahead of print April 24, 2002
Department of Biochemistry, Robert Wood Johnson Medical school, Piscataway, NJ 08854
Corresponding Author: inouye{at}rwja.umdnj.edu
Abstract EnvZ, a histidine kinase/phosphatase in Escherichia coli, responds to the osmolarity changes in the medium by regulating the phosphorylation state of the transcription factor OmpR, which controls the expression levels of outer membrane porin proteins OmpF and OmpC. Although both ompR and envZ genes are located on the ompB locus under the control of the ompB promoter and transcribed as a single polycistronic mRNA, the expression of envZ is known to be significantly less than ompR. However, to date no accurate estimation for amounts of EnvZ and OmpR in the cell has been carried out. Here we examined the levels of EnvZ and OmpR in the wild-type strain MC4100 by quantitative Western blot analysis using anti-OmpR and anti-EnvZc (cytoplasmic domain of EnvZ) antisera. It was observed that during exponential growth in L-broth medium there were approximately 3500 and 100 molecules per cell of OmpR and EnvZ, respectively. The levels of OmpR and EnvZ in MC4100 cells grown in a high osmolarity medium (nutrient broth + 20% sucrose) were about the same as those grown in L-broth, while they are 1.7 fold higher than those in a low osmolarity medium (nutrient broth). With use of His10-OmpR, we also determined the Kd value for the EnvZc-OmpR complex formation to be 1.20 -/+ 0.17 uM. On the basis of these results, the molecular mechanism of osmoregulation of ompF and ompC is discussed.
J. Biol. Chem, 10.1074/jbc.M110715200
Submitted on November 7, 2001
Revised on April 23, 2002
Accepted on April 24, 2002
EnvZ-OmpR interaction and Osmoregulaton in Escherichia coli
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