Interaction of the FimB Integrase with the FimS Invertible DNA Element in Escherichia Coli in Vivo and in Vitro
Overview
Authors
Affiliations
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.
Diversity in Genetic Regulation of Bacterial Fimbriae Assembled by the Chaperone Usher Pathway.
Gahlot D, Taheri N, MacIntyre S Int J Mol Sci. 2023; 24(1).
PMID: 36613605 PMC: 9820224. DOI: 10.3390/ijms24010161.
Blockage of bacterial FimH prevents mucosal inflammation associated with Crohn's disease.
Chevalier G, Laveissiere A, Desachy G, Barnich N, Sivignon A, Maresca M Microbiome. 2021; 9(1):176.
PMID: 34425887 PMC: 8383459. DOI: 10.1186/s40168-021-01135-5.
Battaglioli E, Goh K, Atruktsang T, Schwartz K, Schembri M, Welch R mBio. 2018; 9(4).
PMID: 30087170 PMC: 6083910. DOI: 10.1128/mBio.01360-18.
Temporal Regulation of Genes in Uropathogenic during Infection of the Murine Urinary Tract.
Schwan W, Ding H J Pathog. 2018; 2017:8694356.
PMID: 29445547 PMC: 5763102. DOI: 10.1155/2017/8694356.
Dorman C, Bogue M Sci Prog. 2017; 99(4):420-437.
PMID: 28742481 PMC: 10365484. DOI: 10.3184/003685016X14811202974921.