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J. Biol. Chem., Vol. 276, Issue 47, 43618-43626, November 23, 2001
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From the Department of Biochemistry, University of Illinois at
Urbana-Champaign, Urbana, Illinois 61801
In the Gram-positive soil bacterium
Bacillus subtilis, the chemoreceptors are coupled to the
central two-component kinase CheA via two proteins, CheW and CheV. CheV
is a two-domain protein with an N-terminal CheW-like domain and a
C-terminal two-component receiver domain. In this study, we show that
CheV is phosphorylated in vitro on a conserved aspartate in
the presence of phosphorylated CheA (CheA-P). This reaction is
slower compared with the phospho-transfer reaction between CheA-P and
one other response regulator of the system, CheB. CheV-P is also highly
stable in comparison with CheB-P. Both of these properties are more
pronounced in the full-length protein compared with a truncated form
composed only of the receiver domain, that is, deletion of the
CheW-like domain results in increase in the rate of the
phospho-transfer reaction and decrease in stability of the
phosphorylated protein. Phosphorylation of CheV is required for
adaptation to the addition of the chemoattractant asparagine. In
tethered-cell assays, strains expressing an unphosphorylatable point
mutant of cheV or a truncated mutant lacking the entire receiver domain are severely impaired in adaptation to the addition of
asparagine. Both of these strains, however, show near normal counterclockwise biases, suggesting that in the absence of the attractant the chemoreceptors are efficiently coupled to CheA kinase by
the mutant CheV proteins. Inability of the CheW-like domain of CheV to
support complete adaptation to the addition of asparagine also suggests
that unlike CheW, this domain by itself may lead to the formation of
signaling complexes that stay overactive in the presence of the
attractant. A possible structural basis for this feature is discussed.
Phosphorylation of the Response Regulator CheV Is Required for
Adaptation to Attractants during Bacillus subtilis
Chemotaxis*
*
This work was supported by National Institutes of Health
Grant GM54365 (to G. W. O.).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.: 217-333-9098;
Fax: 217-333-8868; E-mail: g-ordal@uiuc.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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