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Papers In Press, published online ahead of print March 29, 2000
Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, Chapel Hill, NC 27599-7290
Corresponding Author: bourret{at}med.unc.edu
In Escherichia coli, swimming behavior is mediated by the phosphorylation state of the response regulator CheY. In its active, phosphorylated form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. When Ile 95 of CheY is replaced by a valine, increased CW rotation correlates with enhanced binding to FliM. One possible explanation for the hyperactivity of this mutant is that residue 95 affects the conformation of an adjacent tyrosine side chain at position 106, which has been suggested to play a role in a signaling step of CheY subsequent to switch binding. In order to assess this possibility directly, the crystal structure of CheY95IV was determined. Several other mutants with substitutions at position 95 were characterized to establish the structural requirements for switch binding and signaling at this position and to investigate a general relationship between the two properties. The mutations generated affected both rotational behavior and FliM binding. Combined genetic, biochemical, and crystallographic results suggested that residue 95 mediates the surface complementarity between CheY and FliM and also independently affects the conformation of Tyr 106 . The various phenotypes of these mutants, however, can be explained solely by the amount of phosphorylated CheY bound to the switch. It is not necessary to postulate a signaling step subsequent to switch binding that involves Tyr 106 . Implications of these results regarding the current view of CheY signal transduction are discussed.
J. Biol. Chem, 10.1074/jbc.M909908199
Submitted on December 10, 1999
Revised on March 23, 2000
Accepted on March 29, 2000
Correlated switch binding and signaling in bacterial chemotaxis
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