Human- and plant-pathogenic Pseudomonas species produce bacteriocins exhibiting colicin M-like hydrolase activity towards peptidoglycan precursors.

ABSTRACT: Genes encoding proteins that exhibit similarity to the C-terminal domain of Escherichia coli colicin M were identified in the genomes of some Pseudomonas species, namely, P. aeruginosa, P. syringae, and P. fluorescens. These genes were detected only in a restricted number of strains. In P. aeruginosa, for instance, the colicin M homologue gene was located within the ExoU-containing genomic island A, a large horizontally acquired genetic element and virulence determinant. Here we report the cloning of these genes from the three Pseudomonas species and the purification and biochemical characterization of the different colicin M homologues. All of them were shown to exhibit Mg(2+)-dependent diphosphoric diester hydrolase activity toward the two undecaprenyl phosphate-linked peptidoglycan prec

SUBMITTER: Barreteau H 

PROVIDER: S-EPMC2681890 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature