Xis protein binding to the left arm stimulates excision of conjugative transposon Tn916.

Journal of Bacteriology
Kevin M ConnollyR T Clubb

Abstract

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 ((Tn916)Int) and excisionase ((Tn916)Xis) proteins. In this study, we have investigated the role of the (Tn916)Xis protein in stimulating excisive recombination. The functional relevance of (Tn916)Xis 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 (Tn916)Xis 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 (Tn916)Int, suggesting that the (Tn916)Xis 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, def...Continue Reading

References

Dec 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·S D GoodmanH A Nash
Jan 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·L Moitoso de Vargas, A Landy
Jul 1, 1988·Journal of Bacteriology·D B ClewellC Gawron-Burke
Feb 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·S YinA Landy
May 25, 1985·Journal of Molecular Biology·A KikuchiR A Weisberg
Nov 1, 1995·Journal of Bacteriology·D D Jaworski, D B Clewell
Jun 1, 1995·Trends in Microbiology·D B ClewellD D Jaworski
Jan 1, 1994·Biochimie·J ObertoJ Rouvière-Yaniv
Jan 1, 1995·Annual Review of Microbiology·J R Scott, G G Churchward
Apr 1, 1997·Journal of Bacteriology·C K RudyG Churchward
Sep 15, 1997·Nucleic Acids Research·D Esposito, J J Scocca
Oct 10, 1997·Nucleic Acids Research·C RudyG Churchward
Jan 7, 1998·Analytical Biochemistry·M M Ling, B H Robinson
Jul 17, 1998·Nature Structural Biology·K M ConnollyR T Clubb

❮ Previous
Next ❯

Citations

Jul 6, 2010·Nature Reviews. Microbiology·Rachel A F Wozniak, Matthew K Waldor
Aug 4, 2006·Journal of Bacteriology·Sarah M McLeodMatthew K Waldor
Dec 2, 2009·Journal of Bacteriology·Michèle Coddeville, Paul Ritzenthaler
Feb 9, 2007·Proceedings of the National Academy of Sciences of the United States of America·Mohamad A AbbaniRobert T Clubb
Mar 20, 2015·FEMS Microbiology Letters·Rachid MenouniMireille Ansaldi
Nov 20, 2016·Archives of Microbiology·Douglas W Dingman
Apr 4, 2017·FEMS Microbiology Reviews·François DelavatJan Roelof van der Meer
Mar 9, 2019·Microbiology Spectrum·Keith E Weaver

❮ Previous
Next ❯

Related Concepts

Related Feeds

Bacterial Protein Structures

Bacterial protein structures can expedite the development of novel antibiotics. Here is the latest research on bacterial proteins and the resolution of their structures.

Bacterial Protein Structures (ASM)

Bacterial protein structures can expedite the development of novel antibiotics. Here is the latest research on bacterial proteins and the resolution of their structures.