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J. Biol. Chem., Vol. 275, Issue 22, 17080-17085, June 2, 2000
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From the Universität Osnabrück, Fachbereich
Biologie/Chemie, Abteilung Mikrobiologie, D-49069 Osnabrück,
Germany
The putative turgor sensor KdpD is characterized
by a large, N-terminal domain of about 400 amino acids, which is not
found in any other known sensor kinase. Comparison of 12 KdpD sequences from various microorganisms reveals that this part of the kinase is
highly conserved and includes two motifs (Walker A and Walker B) that
are very similar to the classical ATP-binding sites of ATP-requiring
enzymes. By means of photoaffinity labeling with 8-azido-[ The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF213466.
The Hydrophilic N-terminal Domain Complements the
Membrane-anchored C-terminal Domain of the Sensor Kinase KdpD of
Escherichia coli*
,§
-32P]ATP, direct evidence was obtained
for the existence of an ATP-binding site located in the N-terminal
domain of KdpD. The N-terminal domain, KdpD/1-395, was overproduced
and purified. Although predicted to be hydrophilic, it was found to be
membrane-associated and could be solubilized either by treatment with
buffer of low ionic strength or detergent. The membrane-associated
form, but not the solubilized one, retained the ability to bind
8-azido-[-32P]ATP. Previously, it was shown that the
phosphatase activity of a truncated KdpD, KdpD/
12-395, is
deregulated in vitro (Jung, K., and Altendorf, K. (1998)
J. Biol. Chem. 273, 17406-17410). Here, we
demonstrated that this effect was reversed in vesicles containing both
the truncated KdpD and the N-terminal domain. Furthermore, coexpression
of kdpD/12-395 and kdpD/1-395 restored signal transduction in vivo. These results highlight the
importance of the N-terminal domain for the function of KdpD and
provide evidence for an interaction of this domain and the transmitter domain of the sensor kinase.
*
This work was supported by the Deutsche
Forschungsgemeinschaft (SFB 431) and 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.
Recipients of fellowships from the Deutsche
Forschungsgemeinschaft: Heisenberg-Stipendium (to K. J.) and
Graduiertenkolleg (to R. H.).
§
To whom correspondence should be addressed: Universität
Osnabrück, Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, Barbarastr. 11, D-49069 Osnabrück, Germany. Tel.:
49-541-969-2276; Fax: 49-541-969-2870; E-mail: jung_k@biologie.uni-osnabrueck.de.
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