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J. Biol. Chem., Vol. 275, Issue 32, 24264-24272, August 11, 2000
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From the Department of Biochemistry, Colleges of Medicine and
Liberal Arts and Sciences, University of Illinois,
Urbana, Illinois 61801
The Bacillus subtilis McpB is a class
III chemotaxis receptor, from which methanol is released in response to
all stimuli. McpB has four putative methylation sites based upon the
Escherichia coli consensus sequence. To explore the
nature of methanol release from a class III receptor, all combinations
of putative methylation sites Gln371,
Gln595, Glu630, and Glu637 were
substituted with aspartate, a conservative substitution that
effectively eliminates methylation.
McpB(Q371D,E630D,E637D) in a This work is dedicated in loving memory to Jane Tucker Zimmer
(1940-1996).
Selective Methylation Changes on the Bacillus
subtilis Chemotaxis Receptor McpB Promote Adaptation*
(mcpA mcpB tlpA
tlpB)101::cat mcpC4::erm background failed to release methanol in response to either the addition or removal of
the McpB-mediated attractant asparagine. In the same background, McpB(E630D,E637D) produced methanol only upon asparagine
addition, whereas McpB(Q371D,E630D) produced methanol only
upon asparagine removal. Thus methanol release from McpB was selective.
Mutants unable to methylate site 637 but able to methylate site 630 had high prestimulus biases and were incapable of adapting to asparagine addition. Mutants unable to methylate site 630 but able to methylate site 637 had low prestimulus biases and were impaired in adaptation to
asparagine removal. We propose that selective methylation of these two
sites represents a method of adaptation novel from E. coli
and present a model in which a charged residue rests between them. The
placement of this charge would allow for opposing electrostatic effects
(and hence opposing receptor conformational changes). We propose that
CheC, a protein not found in enteric systems, has a role in regulating
this selective methylation.
*
This work was supported by Public Health Service Grant
GM54365 (to G. W. O.) 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.: 217-333-9098 or
217-333-0268; Fax: 217-333-8868; E-mail: g-ordal@uiuc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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