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Interaction of the FimB Integrase with the FimS Invertible DNA Element in Escherichia Coli in Vivo and in Vitro

Overview
Journal J Bacteriol
Specialty Microbiology
Date 2000 Apr 27
PMID 10781567
Citations 10
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Abstract

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.

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References
1.
Pargellis C, de Vargas L, Landy A . Suicide recombination substrates yield covalent lambda integrase-DNA complexes and lead to identification of the active site tyrosine. J Biol Chem. 1988; 263(16):7678-85. View

2.
Cao Y, Hayes F . A newly identified, essential catalytic residue in a critical secondary structure element in the integrase family of site-specific recombinases is conserved in a similar element in eucaryotic type IB topoisomerases. J Mol Biol. 1999; 289(3):517-27. DOI: 10.1006/jmbi.1999.2793. View

3.
Kawula T, Orndorff P . Rapid site-specific DNA inversion in Escherichia coli mutants lacking the histonelike protein H-NS. J Bacteriol. 1991; 173(13):4116-23. PMC: 208061. DOI: 10.1128/jb.173.13.4116-4123.1991. View

4.
Abremski K, Hoess R . Evidence for a second conserved arginine residue in the integrase family of recombination proteins. Protein Eng. 1992; 5(1):87-91. DOI: 10.1093/protein/5.1.87. View

5.
Chen J, Evans B, Yang S, Araki H, Oshima Y, Jayaram M . Functional analysis of box I mutations in yeast site-specific recombinases Flp and R: pairwise complementation with recombinase variants lacking the active-site tyrosine. Mol Cell Biol. 1992; 12(9):3757-65. PMC: 360238. DOI: 10.1128/mcb.12.9.3757-3765.1992. View