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Journal of Bacteriology, May 2000, p. 2953-2959, Vol. 182, No. 10
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Interaction of the FimB Integrase with the fimS Invertible DNA Element in Escherichia coli In Vivo and In Vitro

Lesley S. Burns, Stephen G. J. Smith, and Charles J. Dorman*

Department of Microbiology, Moyne Institute of Preventive Medicine, University of Dublin, Trinity College, Dublin 2, Republic of Ireland

Received 23 December 1999/Accepted 21 February 2000

The FimB protein is a site-specific recombinase that inverts the fimS genetic switch in Escherichia coli. Based on amino acid sequence analysis alone, FimB has been assigned to the integrase family of tyrosine recombinases. We show that amino acid substitutions at positions R47, H141, R144, and Y176, corresponding to highly conserved members of the catalytic motif of integrase proteins, render FimB incapable of inverting the fimS element in vivo. The arginine substitutions reduced the ability of FimB to bind to fimS in vivo or in vitro, while the substitution R144Q resulted in a protein unable to bind independently to the half sites located at the left end of fimS in phase-on bacteria. These data confirm that FimB is an integrase and suggest that residue R144 has a role in binding to a specific component of the fim switch.

* Corresponding author. Mailing address: Department of Microbiology, Moyne Institute of Preventive Medicine, University of Dublin, Trinity College, Dublin 2, Republic of Ireland. Phone: 353 1 608 2013. Fax: 353 1 679 9294. E-mail: cjdorman{at}tcd.ie.

Journal of Bacteriology, May 2000, p. 2953-2959, Vol. 182, No. 10
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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