HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 275, Issue 26, 19752-19758, June 30, 2000

This Article Full Text Full Text (PDF) All Versions of this Article: 275/26/19752    most recent M909908199v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Schuster, M. Articles by Collins, E. J. Search for Related Content PubMed PubMed Citation Articles by Schuster, M. Articles by Collins, E. J. Social Bookmarking                      What's this?

Correlated Switch Binding and Signaling in Bacterial Chemotaxis^*

Martin Schuster, Rui Zhao, Robert B. Bourret, and Edward J. Collins

From the Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, North Carolina 27599-7290

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 Ile⁹⁵ of CheY is replaced by a valine, increased clockwise rotation correlates with enhanced binding to FliM. A possible explanation for the hyperactivity of this mutant is that residue 95 affects the conformation of nearby residues that potentially interact with FliM. In order to assess this possibility directly, the crystal structure of CheY95IV was determined. We found that CheY95IV is structurally almost indistinguishable from wild-type CheY. Several other mutants with substitutions at position 95 were characterized to establish the structural requirements for switch binding and clockwise signaling at this position and to investigate a general relationship between the two properties. The various rotational phenotypes of these mutants can be explained solely by the amount of phosphorylated CheY bound to the switch, which was inferred from the phosphorylation properties of the mutant CheY proteins and their binding affinities to FliM. Combined genetic, biochemical, and crystallographic results suggest that residue 95 itself is critical in mediating the surface complementarity between CheY and FliM.

The atomic coordinates and the structure factors (code 1D4Z) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				M. C. Lane, A. N. Simms, and H. L. T. Mobley Complex Interplay between Type 1 Fimbrial Expression and Flagellum-Mediated Motility of Uropathogenic Escherichia coli J. Bacteriol., August 1, 2007; 189(15): 5523 - 5533. [Abstract] [Full Text] [PDF]

				S. L. Porter, G. H. Wadhams, A. C. Martin, E. D. Byles, D. E. Lancaster, and J. P. Armitage The CheYs of Rhodobacter sphaeroides J. Biol. Chem., October 27, 2006; 281(43): 32694 - 32704. [Abstract] [Full Text] [PDF]

				K. I. Varughese Conformational Changes of Spo0F along the Phosphotransfer Pathway J. Bacteriol., December 15, 2005; 187(24): 8221 - 8227. [Abstract] [Full Text] [PDF]

				H. Szurmant and G. W. Ordal Diversity in Chemotaxis Mechanisms among the Bacteria and Archaea Microbiol. Mol. Biol. Rev., June 1, 2004; 68(2): 301 - 319. [Abstract] [Full Text] [PDF]

				J. G. Smith, J. A. Latiolais, G. P. Guanga, S. Citineni, R. E. Silversmith, and R. B. Bourret Investigation of the Role of Electrostatic Charge in Activation of the Escherichia coli Response Regulator CheY J. Bacteriol., November 1, 2003; 185(21): 6385 - 6391. [Abstract] [Full Text] [PDF]

				R. E. Silversmith, G. P. Guanga, L. Betts, C. Chu, R. Zhao, and R. B. Bourret CheZ-Mediated Dephosphorylation of the Escherichia coli Chemotaxis Response Regulator CheY: Role for CheY Glutamate 89 J. Bacteriol., March 1, 2003; 185(5): 1495 - 1502. [Abstract] [Full Text] [PDF]

				S. D. Re, T. Tolstykh, P. M. Wolanin, and J. B. Stock Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism Protein Sci., November 1, 2002; 11(11): 2644 - 2654. [Abstract] [Full Text] [PDF]

				Y. J. Im, S.-H. Rho, C.-M. Park, S.-S. Yang, J.-G. Kang, J. Y. Lee, P.-S. Song, and S. H. Eom Crystal structure of a cyanobacterial phytochrome response regulator Protein Sci., March 1, 2002; 11(3): 614 - 624. [Abstract] [Full Text] [PDF]

				A. Bren and M. Eisenbach How Signals Are Heard during Bacterial Chemotaxis: Protein-Protein Interactions in Sensory Signal Propagation J. Bacteriol., December 15, 2000; 182(24): 6865 - 6873. [Full Text]

				R. E. Silversmith, J. G. Smith, G. P. Guanga, J. T. Les, and R. B. Bourret Alteration of a Nonconserved Active Site Residue in the Chemotaxis Response Regulator CheY Affects Phosphorylation and Interaction with CheZ J. Biol. Chem., May 18, 2001; 276(21): 18478 - 18484. [Abstract] [Full Text] [PDF]

				M. Schuster, R. E. Silversmith, and R. B. Bourret Conformational coupling in the chemotaxis response regulator CheY PNAS, May 22, 2001; 98(11): 6003 - 6008. [Abstract] [Full Text] [PDF]