JBC Transcription and Nuclear Factor Monoclonals

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Originally published In Press as doi:10.1074/jbc.M107881200 on October 30, 2001

J. Biol. Chem., Vol. 276, Issue 52, 49449-49458, December 28, 2001
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Inhibition of the Agrobacterium tumefaciens TraR Quorum-sensing Regulator
INTERACTIONS WITH THE TraM ANTI-ACTIVATOR*

Anna SwiderskaDagger , Amy K. BerndtsonDagger , Mee-Rye ChaDagger , Lina LiDagger , Gerard M. J. Beaudoin IIIDagger §, Jun Zhu||, and Clay FuquaDagger **

From the Dagger  Department of Biology, Indiana University, Bloomington, Indiana 47405 and  Section of Microbiology, Cornell University, Ithaca, New York 14853

The Agrobacterium tumefaciens quorum-sensing transcriptional regulator TraR and its inducing ligand 3-oxo-octanoyl-L-homoserine lactone control conjugal transfer of the tumor-inducing plasmid, the primary virulence factor responsible for crown gall disease of plants. This regulatory system enables A. tumefaciens to express its conjugal transfer regulon preferentially at high population densities. TraR activity is antagonized by a second tumor-inducing plasmid-encoded protein designated TraM. TraM and TraR are thought to form an anti-activation complex that prevents TraR from recognizing its target DNA-binding sites. The formation and inhibitory function of the TraM-TraR anti-activation complex was analyzed using several different assays for protein-protein interaction, including surface plasmon resonance. The TraR-TraM complex forms readily in solution and is extremely stable (KD of 1-4 × 10-9 M). Directed mutational analysis of TraM identified a number of amino acids that play important roles in the inhibition of TraR, clustering in two regions of the protein. Interestingly, several mutants were identified that proficiently bound TraR but were unable to inhibit its activity. This observation suggests a mechanistic separation between the initial assembly of the complex and conversion of TraR to an inactive form.

* This work was supported by Grant MCB-9974863 from the National Science Foundation (to C. F.) and NIGMS Grant GM42893 from the National Institutes of Health (to S. C. Winans).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.

§ Current address: Dept. of Neuroscience, The Johns Hopkins University, Baltimore, MD 21211.

|| Current address: Dept. of Microbiology and Molecular Genetics, Harvard Medical School, Bldg. D1, 200 Longwood Ave., Boston, MA 02115.

** To whom correspondence should be addressed: Dept. of Biology, Jordan Hall 142, 1001 E. 3rd St., Indiana University, Bloomington, IN 47405-1847. Tel.: 812-856-6005; Fax: 812-855-6705; E-mail: cfuqua@bio.indiana.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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