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J. Biol. Chem., Vol. 275, Issue 51, 40142-40147, December 22, 2000
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From the The membrane-bound histidine kinase KdpD is a
putative turgor sensor that regulates, together with the response
regulator KdpE, the expression of the kdpFABC operon coding
for the high affinity K+-uptake system KdpFABC of
Escherichia coli. To elucidate the nature of the primary
stimulus for KdpD, we developed an in vitro assay based on
right-side-out membrane vesicles. Conditions were varied inside
and outside of the vesicles, and KdpD autophosphorylation activity was
tested. It was shown that an increase of the ionic strength inside the
vesicles was accompanied by an increase of the autophosphorylation
activity of KdpD with ATP. However, K+ at concentrations
higher than 1 mM inhibited KdpD autophosphorylation activity. This K+-specific effect was not observed with
KdpD-Arg-511
K+ and Ionic Strength Directly Influence the
Autophosphorylation Activity of the Putative Turgor Sensor KdpD of
Escherichia coli*
§,¶, and
Universität Osnabrück,
Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, D-49069
Osnabrück, and the ¶ Technische Universität Berlin,
Institut für Biotechnologie, Fachgebiet Mikrobiologie und
Genetik, D-13355 Berlin, Germany
Gln, a KdpD derivative, which causes
K+-independent kdpFABC expression. When the
osmolality outside the vesicles was increased, autophosphorylation
activity of KdpD was stimulated, whereby salts were more effective than
sugars. Treatment of the vesicles with amphipathic compounds did not
affect KdpD autophosphorylation activity. Based on these results it is
proposed that changes of intracellular parameters elicited by
K+ limitation or osmotic upshock directly influence KdpD
autophosphorylation activity, whereby K+ has an inhibitory
and ionic strength a stimulatory effect.
*
This work was supported by the Deutsche
Forschungsgemeinschaft (SFB 431, JU 270/3-1) and by the Fonds der
Chemischen Industrie.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.
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