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Journal of Bacteriology, October 1998, p. 5102-5108, Vol. 180, No. 19
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Expression of the Kdp ATPase Is Consistent with
Regulation by Turgor Pressure
Ravi
Malli and
Wolfgang
Epstein*
Department of Molecular Genetics and Cell
Biology, The University of Chicago, Chicago, Illinois 60637
Received 4 February 1998/Accepted 3 August 1998
The kdpFABC operon of Escherichia coli
encodes the four protein subunits of the Kdp K+ transport
system. Kdp is expressed when growth is limited by the availability of
K+. Expression of Kdp is dependent on the products of the
adjacent kdpDE operon, which encodes a pair of
two-component regulators. Studies with kdp-lac fusions led
to the suggestion that change in turgor pressure acts as the signal to
express Kdp (L. A. Laimins, D. B. Rhoads, and W. Epstein,
Proc. Natl. Acad. Sci. USA 78:464-468, 1981). More recently, effects
of compatible solutes, among others, have been interpreted as
inconsistent with the turgor model (H. Asha and J. Gowrishankar, J. Bacteriol. 175:4528-4537, 1993). We re-examined the effects of
compatible solutes and of medium pH on expression of Kdp in studies in
which growth rate was also measured. In all cases, Kdp expression
correlated with the K+ concentration when growth began to
slow. Making the reasonable but currently untestable assumptions that
the reduction in growth rate by K+ limitation is due to a
reduction in turgor and that addition of betaine does not increase
turgor, we concluded that all of the data on Kdp expression are
consistent with control by turgor pressure.
*
Corresponding author. Mailing address: Department of
Molecular Genetics and Cell Biology, The University of Chicago, 920 E. 58th St., Chicago, IL 60637. Phone: (773) 702-1331. Fax: (773) 702-3172. E-mail: wepstein{at}midway.uchicago.edu.
Journal of Bacteriology, October 1998, p. 5102-5108, Vol. 180, No. 19
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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