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Updated: Feb 14, 2026

Super-resolution Imaging of Proteus mirabilis Biofilm by Expansion Microscopy
Published on: July 18, 2025
The XerC recombinase of Proteus mirabilis: characterization and interaction with other tyrosine recombinases
Manuela Villion1, George Szatmari
1Département de microbiologie et immunologie, Université de Montréal, CP 6128, Succ. Centre-Ville, H3C 3J7, Montreal, QC, Canada.
Abstract:
XerC and XerD are two site-specific recombinases, which act on different sites to maintain replicons in a monomeric state. This system, which was first discovered and studied in Escherichia coli, is present in several species including Proteus mirabilis, where the XerD recombinase was previously characterized by our laboratory. In this paper, we report the presence of the xerC gene in P. mirabilis. Using in vitro reactions, we show that the two P. mirabilis recombinases display binding and cleavage activity on the E. coli dif site and the ColE1 cer site, together or in collaboration with E. coli recombinases. In vivo, P. mirabilis XerC and XerD are able to resolve and monomerize a plasmid containing two cer sites, increasing its stability. However, P. mirabilis XerC, in combination with E. coli XerD, is unable to perform these functions.
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