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Journal of Bacteriology, June 2009, p. 3657-3664, Vol. 191, No. 11
0021-9193/09/$08.00+0     doi:10.1128/JB.01824-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Human- and Plant-Pathogenic Pseudomonas Species Produce Bacteriocins Exhibiting Colicin M-Like Hydrolase Activity towards Peptidoglycan Precursors{triangledown}

Hélène Barreteau,1,2 Ahmed Bouhss,1,2 Martine Fourgeaud,3,4,5 Jean-Luc Mainardi,3,4,5 Thierry Touzé,1,2 Fabien Gérard,1,2 Didier Blanot,1,2 Michel Arthur,3,4,5 and Dominique Mengin-Lecreulx1,2*

Université Paris-Sud, Institut de Biochimie et Biophysique Moléculaire et Cellulaire, UMR 8619, Orsay F-91405, France,1 CNRS, Laboratoire des Enveloppes Bactériennes et Antibiotiques, UMR 8619, Orsay F-91405, France,2 Centre de Recherche des Cordeliers, LRMA, Equipe 12, Université Pierre et Marie Curie, UMR-S 872, Paris F-75006, France,3 Université Paris Descartes, UMR-S 872, Paris F-75006, France,4 INSERM, U872, Paris F-75006, France5

Received 25 December 2008/ Accepted 24 March 2009

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 Mg2+-dependent diphosphoric diester hydrolase activity toward the two undecaprenyl phosphate-linked peptidoglycan precursors (lipids I and II) in vitro. In all cases, the site of cleavage was localized between the undecaprenyl and pyrophospho-MurNAc moieties of these precursors. These enzymes were not active on the cytoplasmic precursor UDP-MurNAc-pentapeptide or (or only very poorly) on undecaprenyl pyrophosphate. These colicin M homologues have a narrow range of antibacterial activity. The P. aeruginosa protein at low concentrations was shown to inhibit growth of sensitive P. aeruginosa strains. These proteins thus represent a new class of bacteriocins (pyocins), the first ones reported thus far in the genus Pseudomonas that target peptidoglycan metabolism.

* Corresponding author. Mailing address: Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, UMR 8619, CNRS, Université Paris-Sud, Bâtiment 430, 91405 Orsay Cedex, France. Phone: 33-1-69-15-48-41. Fax: 33-1-69-85-37-15. E-mail: dominique.mengin-lecreulx{at}u-psud.fr

{triangledown} Published ahead of print on 3 April 2009.

Journal of Bacteriology, June 2009, p. 3657-3664, Vol. 191, No. 11
0021-9193/09/$08.00+0     doi:10.1128/JB.01824-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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