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Characterization of colicin M and its orthologs targeting bacterial cell wall peptidoglycan biosynthesis. 2012
Hélène Barreteau, and
Meriem El Ghachi, and
Aurélie Barnéoud-Arnoulet, and
Emmanuelle Sacco, and
Thierry Touzé, and
Denis Duché, and
Fabien Gérard, and
Mark Brooks, and
Delphine Patin, and
Ahmed Bouhss, and
Didier Blanot, and
Herman van Tilbeurgh, and
Michel Arthur, and
Roland Lloubès, and
Dominique Mengin-Lecreulx
Institut de Biochimie et Biophysique Moléculaire et Cellulaire, Université Paris-Sud , UMR 8619 CNRS, Orsay, France.
For a long time, colicin M was known for killing susceptible Escherichia coli cells by interfering with cell wall peptidoglycan biosynthesis, but its precise mode of action was only recently elucidated: this bacterial toxin was demonstrated to be an enzyme that catalyzes the specific degradation of peptidoglycan lipid intermediate II, thereby provoking the arrest of peptidoglycan synthesis and cell lysis. The discovery of this activity renewed the interest in this colicin and opened the way for biochemical and structural analyses of this new class of enzyme (phosphoesterase). The identification of a few orthologs produced by pathogenic strains of Pseudomonas further enlarged the field of investigation. The present article aims at reviewing recently acquired knowledge on the biology of this small family of bacteriocins.
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