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J. Biol. Chem., Vol. 277, Issue 27, 24155-24161, July 5, 2002
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From the Department of Biochemistry, Robert Wood Johnson Medical
School, Piscataway, New Jersey 08854
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 the 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
~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 with 20% sucrose) were about the
same as those grown in L-broth, whereas they were 1.7-fold higher than
those in a low osmolarity medium (nutrient broth). With
His10-OmpR, we also determined that the
Kd value for the EnvZc-OmpR complex formation is
1.20 ± 0.17 µM. On the basis of these results, the
molecular mechanism of osmoregulation of ompF and
ompC is discussed.
EnvZ-OmpR Interaction and Osmoregulation in Escherichia
coli*
*
This work was supported by Grant GM19043 from the National
Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 732-235-4115;
Fax: 732-235-4559; E-mail: inouye@rwja.umdnj.edu.
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