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Volume 272, Number 38, Issue of September 19, 1997 pp. 23758-23764
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The CheZ-binding Surface of CheY Overlaps the CheA- and FliM-binding Surfaces

(Received for publication, April 25, 1997, and in revised form, July 2, 1997)

From the Department of Microbiology and Immunology, University of Illinois, Chicago, Illinois 60612

CheY, the response regulator of bacterial chemotaxis, plays a pivotal role in signal transduction in bacterial chemotaxis and interacts with at least three proteins: CheA, FliM, and CheZ. CheA receives signals from chemoreceptors and then transfers the signal to CheY by a phosphotransfer reaction. Phosphorylated CheY binds to FliM, one of the switch proteins, resulting in a change in flagellar rotation from counterclockwise to clockwise. Phosphorylated CheY is dephosphorylated by its intrinsic autophosphatase activity and by CheZ. The CheA- and FliM-binding surfaces of CheY have been well studied, but characterization of the CheZ-binding surface of CheY is incomplete. We have analyzed the effect of CheZ on the dephosphorylation rates of 14 mutants of CheY. Nine mutant CheY proteins showed more resistance to CheZ phosphatase activity than did wild-type CheY. These nine mutant CheY proteins could be divided into two groups: one with altered CheZ binding and the other with normal CheZ binding. The mutations causing reduced CheZ binding altered residues on the same surface of CheY, a region consisting of the ₅-₅ loop, the ₁-helix, and part of the ₅-helix. Mutations rendering CheY resistant to CheZ, isolated by Sanna et al. (Sanna, M. G., Swanson, R. V., Bourret, R. B., and Simon, M. I. (1995) Mol. Microbiol. 15, 1069-1079), were also found to affect this surface. The mutations in the CheY protein that affect CheZ activity but not CheZ binding are located in the ₄-₄ loop, which appears to be involved in the catalytic activity of CheZ. Finally, our results indicate that the CheY surfaces that bind CheA, FliM, and CheZ overlap, but are not completely identical.

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