Related Experiment Video
Updated: May 23, 2026

Isolation and Preparation of Bacterial Cell Walls for Compositional Analysis by Ultra Performance Liquid Chromatography
Published on: January 15, 2014
Characterization of colicin M and its orthologs targeting bacterial cell wall peptidoglycan biosynthesis
Hélène Barreteau1, Meriem El Ghachi, Aurélie Barnéoud-Arnoulet
1Institut de Biochimie et Biophysique Moléculaire et Cellulaire, Université Paris-Sud , UMR 8619 CNRS, Orsay, France.
Abstract:
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.
Insights
Colicin M is a bacterial toxin that kills E. coli by degrading peptidoglycan lipid intermediate II. This enzyme activity, a phosphoesterase, halts cell wall synthesis and causes cell lysis, renewing interest in this bacteriocin family.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Colicin M is a bacteriocin known to inhibit cell wall peptidoglycan biosynthesis in susceptible Escherichia coli.
- Its precise mechanism of action was recently identified, revealing it as an enzyme.
Purpose of the Study:
- To review recent advancements in understanding the biology of colicin M and its orthologs.
- To highlight the enzyme activity and structural characteristics of this class of bacteriocins.
Main Methods:
- Biochemical analyses to characterize the enzymatic activity of colicin M.
- Structural analyses to determine the three-dimensional structure of colicin M.
- Bioinformatic approaches to identify and analyze colicin M orthologs in other bacterial species.
Main Results:
- Colicin M acts as a phosphoesterase, specifically degrading peptidoglycan lipid intermediate II.
- This degradation arrests peptidoglycan synthesis, leading to cell lysis.
- Orthologs of colicin M have been identified in pathogenic Pseudomonas strains.
Conclusions:
- The elucidation of colicin M's enzymatic activity has opened new avenues for research.
- Colicin M represents a novel class of enzymes with implications for understanding bacterial cell wall synthesis and developing new antimicrobial strategies.
- The study of colicin M and its orthologs contributes to the broader field of bacteriocin research.
Related Concept Videos
Inhibitors of Gram-positive Cell Wall Synthesis
Bacterial Cell Wall
Cytoskeletal Proteins in Bacteria
Archaeal Cell Wall
Peptidoglycan Synthesis
Bacterial Phylum Tenericutes

