Document Detail

Characterization of Colicin M and its Orthologs Targeting Bacterial Cell Wall Peptidoglycan Biosynthesis.
MedLine Citation:
PMID:  22432709     Owner:  NLM     Status:  Publisher    
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.
Hélène Barreteau; Meriem El Ghachi; Aurélie Barnéoud-Arnoulet; Emmanuelle Sacco; Thierry Touzé; Denis Duché; Fabien Gérard; Mark Brooks; Delphine Patin; Ahmed Bouhss; Didier Blanot; Herman van Tilbeurgh; Michel Arthur; Roland Lloubès; Dominique Mengin-Lecreulx
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-3-20
Journal Detail:
Title:  Microbial drug resistance (Larchmont, N.Y.)     Volume:  -     ISSN:  1931-8448     ISO Abbreviation:  -     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-3-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9508567     Medline TA:  Microb Drug Resist     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
1 Institut de Biochimie et Biophysique Moléculaire et Cellulaire, Université Paris-Sud , UMR 8619 CNRS, Orsay, France .
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