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J. Biol. Chem., Vol. 281, Issue 32, 22761-22772, August 11, 2006

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Colicin M Exerts Its Bacteriolytic Effect via Enzymatic Degradation of Undecaprenyl Phosphate-linked Peptidoglycan Precursors^*

From the Laboratoire des Enveloppes Bactériennes et Antibiotiques, UMR 8619 CNRS, Université Paris-Sud, 91405 Orsay, France

Colicin M was earlier demonstrated to provoke Escherichia coli cell lysis via inhibition of cell wall peptidoglycan (murein) biosynthesis. As the formation of the O-antigen moiety of lipopolysaccharides was concomitantly blocked, it was hypothesized that the metabolism of undecaprenyl phosphate, an essential carrier lipid shared by these two pathways, should be the target of this colicin. However, the exact target and mechanism of action of colicin M was unknown. Colicin M was now purified to near homogeneity, and its effects on cell wall peptidoglycan metabolism reinvestigated. It is demonstrated that colicin M exhibits both in vitro and in vivo enzymatic properties of degradation of lipid I and lipid II peptidoglycan intermediates. Free undecaprenol and either 1-pyrophospho-MurNAc-pentapeptide or 1-pyrophospho-MurNAc-(pentapeptide)-Glc-NAc were identified as the lipid I and lipid II degradation products, respectively, showing that the cleavage occurred between the lipid moiety and the pyrophosphoryl group. This is the first time such an activity is described. Neither undecaprenyl pyrophosphate nor the peptidoglycan nucleotide precursors were substrates of colicin M, indicating that both undecaprenyl and sugar moieties were essential for activity. The bacteriolytic effect of colicin M therefore appears to be the consequence of an arrest of peptidoglycan polymerization steps provoked by enzymatic degradation of the undecaprenyl phosphate-linked peptidoglycan precursors.

Received for publication, March 27, 2006 , and in revised form, June 14, 2006.

^* This work was supported by Grants from the European Community (FP6, COBRA project, LSHM-CT-2003-503-335) and from the Centre National de la Recherche Scientifique (UMR 8619). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Recipient of a scholarship from the Ministère de l'Education Nationale, de la Recherche et de la Technologie (Ecole Doctorale Innovation Thérapeutique, du Fondamental à l'Appliqué).

² Supported by the European Community.

³ To whom correspondence should be addressed: Laboratoire des Enveloppes Bactériennes et Antibiotiques, IBBMC, UMR8619 CNRS, Université Paris-Sud, Bâtiment 430, 91405 Orsay Cedex, France. Tel.: 33-1-69-15-48-41; Fax: 33-1-69-85-37-15; E-mail: dominique.mengin-lecreulx{at}ebp.u-psud.fr.

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