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Journal of Bacteriology, April 2002, p. 2088-2099, Vol. 184, No. 8
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.8.2088-2099.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Xis Protein Binding to the Left Arm Stimulates Excision of Conjugative Transposon Tn916

Kevin M. Connolly, Mizuho Iwahara, and Robert T. Clubb*

Department of Chemistry and Biochemistry, UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, and the Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California 90095-1570

Received 9 October 2001/ Accepted 20 January 2002

Tn916 and related conjugative transposons are clinically significant vectors for the transfer of antibiotic resistance among human pathogens, and they excise from their donor organisms using the transposon-encoded integrase (Tn916Int) and excisionase (Tn916Xis) proteins. In this study, we have investigated the role of the Tn916Xis protein in stimulating excisive recombination. The functional relevance of Tn916Xis binding sites on the arms of the transposon has been assessed in vivo using a transposon excision assay. Our results indicate that in Escherichia coli the stimulatory effect of the Tn916Xis protein is mediated by sequence-specific binding to either of its two binding sites on the left arm of the transposon. These sites lie in between the core and arm sites recognized by Tn916Int, suggesting that the Tn916Xis protein enhances excision in a manner similar to the excisionase protein of bacteriophage {lambda}, serving an architectural role in the stabilization of protein-nucleic acid structures required for strand synapsis. However, our finding that excision in E. coli is significantly enhanced by the host factor HU, but does not depend on the integration host factor or the factor for inversion stimulation, defines clear mechanistic differences between Tn916 and bacteriophage {lambda} recombination.

* Corresponding author. Mailing address: Dept. of Chemistry and Biochemistry, DOE Laboratory of Structural Biology and Molecular Medicine, 405 Hilgard Ave., Los Angeles, CA 90095-1570. Phone: (310) 206-2334. Fax: (310) 206-4749. E-mail: rclubb{at}mbi.ucla.edu.

Journal of Bacteriology, April 2002, p. 2088-2099, Vol. 184, No. 8
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.8.2088-2099.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Abbani, M. A., Papagiannis, C. V., Sam, M. D., Cascio, D., Johnson, R. C., Clubb, R. T. (2007). Structure of the cooperative Xis-DNA complex reveals a micronucleoprotein filament that regulates phage lambda intasome assembly. Proc. Natl. Acad. Sci. USA 104: 2109-2114 [Abstract] [Full Text]  
  • McLeod, S. M., Burrus, V., Waldor, M. K. (2006). Requirement for Vibrio cholerae Integration Host Factor in Conjugative DNA Transfer.. J. Bacteriol. 188: 5704-5711 [Abstract] [Full Text]  


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