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

This Article Full Text Full Text (PDF) 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 Zhu, X. Articles by Volz, K. Search for Related Content PubMed PubMed Citation Articles by Zhu, X. Articles by Volz, K. Social Bookmarking                      What's this?

Volume 272, Number 8, Issue of February 21, 1997 pp. 5000-5006
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Crystal Structures of CheY Mutants Y106W and T87I/Y106W
CheY ACTIVATION CORRELATES WITH MOVEMENT OF RESIDUE 106

(Received for publication, August 23, 1996, and in revised form, December 11, 1996)

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

Position 106 in CheY is highly conserved as an aromatic residue in the response regulator superfamily. In the structure of the wild-type, apo-CheY, Tyr¹⁰⁶ is a rotamer whose electron density is observed in both the inside and the outside positions. In the structure of the T87I mutant of CheY, the threonine to isoleucine change at position 87 causes the side chain of Tyr¹⁰⁶ to be exclusively restricted to the outside position. In this report we demonstrate that the T87I mutation causes cells to be smooth swimming and non-chemotactic. We also show that another CheY mutant, Y106W, causes cells to be more tumbly than wild-type CheY, and impairs chemotaxis. In the structure of Y106W, the side chain of Trp¹⁰⁶ stays exclusively in the inside position. Furthermore, a T87I/Y106W double mutant, which confers the same phenotype as T87I, restricts the side chain of Trp¹⁰⁶ to the outside position. The results from these behavioral and structural studies indicate that the rotameric nature of the Tyr¹⁰⁶ residue is involved in activation of the CheY molecule. Specifically, CheY's signaling ability correlates with the conformational heterogeneity of the Tyr¹⁰⁶ side chain. Our data also suggest that these mutations affect the signal at an event subsequent to phosphorylation.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. H. Knaggs, F. R. Salsbury Jr., M. H. Edgell, and J. S. Fetrow Insights into Correlated Motions and Long-Range Interactions in CheY Derived from Molecular Dynamics Simulations Biophys. J., March 15, 2007; 92(6): 2062 - 2079. [Abstract] [Full Text] [PDF]

				A. M. Stock and J. Guhaniyogi A New Perspective on Response Regulator Activation J. Bacteriol., November 1, 2006; 188(21): 7328 - 7330. [Full Text] [PDF]

				E. Nowak, S. Panjikar, P. Konarev, D. I. Svergun, and P. A. Tucker The Structural Basis of Signal Transduction for the Response Regulator PrrA from Mycobacterium tuberculosis J. Biol. Chem., April 7, 2006; 281(14): 9659 - 9666. [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]

				A. Ferre, J. de la Mora, T. Ballado, L. Camarena, and G. Dreyfus Biochemical Study of Multiple CheY Response Regulators of the Chemotactic Pathway of Rhodobacter sphaeroides J. Bacteriol., August 1, 2004; 186(15): 5172 - 5177. [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]

				P. Roche, L. Mouawad, D. Perahia, J.-P. Samama, and D. Kahn Molecular dynamics of the FixJ receiver domain: movement of the {beta}4-{alpha}4 loop correlates with the in and out flip of Phe101 Protein Sci., November 1, 2002; 11(11): 2622 - 2630. [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]

				V. Guillet, N. Ohta, S. Cabantous, A. Newton, and J.-P. Samama Crystallographic and Biochemical Studies of DivK Reveal Novel Features of an Essential Response Regulator in Caulobacter crescentus J. Biol. Chem., October 25, 2002; 277(44): 42003 - 42010. [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]

				J. L. Appleby and R. B. Bourret Proposed Signal Transduction Role for Conserved CheY Residue Thr87, a Member of the Response Regulator Active-Site Quintet J. Bacteriol., July 15, 1998; 180(14): 3563 - 3569. [Abstract] [Full Text]

				M. M. McEvoy, A. C. Hausrath, G. B. Randolph, S. J. Remington, and F. W. Dahlquist Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway PNAS, June 23, 1998; 95(13): 7333 - 7338. [Abstract] [Full Text] [PDF]

				R. Ramakrishnan, M. Schuster, and R. B. Bourret Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY PNAS, April 28, 1998; 95(9): 4918 - 4923. [Abstract] [Full Text] [PDF]

				S. Djordjevic, P. N. Goudreau, Q. Xu, A. M. Stock, and A. H. West Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain PNAS, February 17, 1998; 95(4): 1381 - 1386. [Abstract] [Full Text] [PDF]

				X. Zhu, K. Volz, and P. Matsumura The CheZ-binding Surface of CheY Overlaps the CheA- and FliM-binding Surfaces J. Biol. Chem., September 19, 1997; 272(38): 23758 - 23764. [Abstract] [Full Text] [PDF]

				M. Jiang, R. B. Bourret, M. I. Simon, and K. Volz Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis. THE 2.3 A STRUCTURE OF AN ASPARTATE TO LYSINE MUTANT AT POSITION 13 OF CheY J. Biol. Chem., May 2, 1997; 272(18): 11850 - 11855. [Abstract] [Full Text] [PDF]

				M. Simonovic and K. Volz A Distinct Meta-active Conformation in the 1.1-A Resolution Structure of Wild-type ApoCheY J. Biol. Chem., July 27, 2001; 276(31): 28637 - 28640. [Abstract] [Full Text] [PDF]

				S.-Y. Lee, Ho. S. Cho, J. G. Pelton, D. Yan, E. A. Berry, and D. E. Wemmer Crystal Structure of Activated CheY. COMPARISON WITH OTHER ACTIVATED RECEIVER DOMAINS J. Biol. Chem., May 4, 2001; 276(19): 16425 - 16431. [Abstract] [Full Text] [PDF]

				M. Schuster, R. Zhao, R. B. Bourret, and E. J. Collins Correlated Switch Binding and Signaling in Bacterial Chemotaxis J. Biol. Chem., June 23, 2000; 275(26): 19752 - 19758. [Abstract] [Full Text] [PDF]