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Originally published In Press as doi:10.1074/jbc.M210035200 on February 4, 2003

J. Biol. Chem., Vol. 278, Issue 15, 13173-13182, April 11, 2003
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Mutational Analysis of TraR
CORRELATING FUNCTION WITH MOLECULAR STRUCTURE OF A QUORUM-SENSING TRANSCRIPTIONAL ACTIVATOR*

Zhao-Qing LuoDagger §, Audra J. SmythDagger , Ping GaoDagger , Yinping QinDagger , and Stephen K. FarrandDagger ||

From the Departments of Dagger  Crop Sciences and  Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801

TraR, the quorum-sensing activator of the Agrobacterium tumefaciens Ti plasmid conjugation system, induces gene expression in response to its quormone, N-(3-oxooctanoyl)-L-homoserine lactone. Ligand binding results in dimerization of TraR and is required for its activity. Analysis of N- and C-terminal deletion mutants of TraR localized the quormone-binding domain to a region between residues 39 and 140 and the primary dimerization domain to a region between residues 119 and 156. The dominant-negative properties of these mutants predicted a second dimerization domain at the C terminus of the protein. Analysis of fusions of N-terminal fragments of TraR to lambda cI' confirmed the dimerization activity of these two domains. Fifteen single amino acid substitution mutants of TraR defective in dimerization were isolated. According to the analysis of these mutants, Asp-70 and Gly-113 are essential for quormone binding, whereas Ala-38 and Ala-105 are important, but not essential. Additional residues located within the N-terminal half of TraR, including three located in alpha -helix 9, contribute to dimerization, but are not required for ligand binding. These results and the recently reported crystal structure of TraR are consistent with and complement each other and together define some of the structural and functional relationships of this quorum-sensing activator.

* This work was supported by National Institutes of Health Grant R01 GM52465 (to S. K. F.).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.

§ Present address: Dept. of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02148.

|| To whom correspondence should be addressed: Dept. of Crop Sciences, University of Illinois at Urbana-Champaign, 240 ERML, 1201 West Gregory Dr., Urbana, IL 61801. Tel.: 217-333-1524; Fax: 217-244-7830; E-mail: stephenf@uiuc.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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