ArticleThe Journal of biological chemistry2010
Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 44 citations in OpenAlex.
- Pyocins and Beyond: Exploring the World of Bacteriocins in Pseudomonas aeruginosa.Probiotics and antimicrobial proteins · 2025Review
- Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system.FEBS open bio · 2024Article
- Colicins and Microcins Produced byInternational journal of environmental research and public health · 2022Review
- Reprogramming microbial populations using a programmed lysis system to improve chemical production.Nature communications · 2021Article
- The Biology of Colicin M and Its Orthologs.Antibiotics (Basel, Switzerland) · 2021Review
- CbrA Mediates Colicin M Resistance in Escherichia coli through Modification of Undecaprenyl-Phosphate-Linked Peptidoglycan Precursors.Journal of bacteriology · 2020Article
- Pseudomonas bacteriocin syringacin M released upon desiccation suppresses the growth of sensitive bacteria in plant necrotic lesions.Microbial biotechnology · 2020Article
- Impact of FiuA Outer Membrane Receptor Polymorphism on the Resistance ofJournal of bacteriology · 2019Article
- A Colicin M-Type Bacteriocin from Pseudomonas aeruginosa Targeting the HxuC Heme Receptor Requires a Novel Immunity Partner.Applied and environmental microbiology · 2018Article
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- A Natural ChimericmBio · 2017Article
- Article
- Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression.Antibiotics (Basel, Switzerland) · 2016Article
- Distinct colicin M-like bacteriocin-immunity pairs in Burkholderia.Scientific reports · 2015Article
- Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis.Science (New York, N.Y.) · 2014Article
- Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake.Molecular microbiology · 2014Article
- Global transcriptional responses to the bacteriocin colicin M in Escherichia coli.BMC microbiology · 2013Article
- The crystal structure of the lipid II-degrading bacteriocin syringacin M suggests unexpected evolutionary relationships between colicin M-like bacteriocins.The Journal of biological chemistry · 2012Article
- Functional and structural characterization of PaeM, a colicin M-like bacteriocin produced by Pseudomonas aeruginosa.The Journal of biological chemistry · 2012Article
- CbrA is a flavin adenine dinucleotide protein that modifies the Escherichia coli outer membrane and confers specific resistance to Colicin M.Journal of bacteriology · 2012Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Colicin M inhibits Escherichia coli peptidoglycan synthesis through cleavage of its lipid-linked precursors. It has a compact structure, whereas other related toxins are organized in three independent domains, each devoted to a particular function: translocation through the outer membrane, receptor binding, and toxicity, from the N to the C termini, respectively. To establish whether colicin M displays such an organization despite its structural characteristics, protein dissection experiments were performed, which allowed us to delineate an independent toxicity domain encompassing exactly the C-terminal region conserved among colicin M-like proteins and covering about half of colicin M (residues 124-271). Surprisingly, the in vitro activity of the isolated domain was 45-fold higher than that of the full-length protein, suggesting a mechanism by which the toxicity of this domain is revealed following primary protein maturation. In vivo, the isolated toxicity domain appeared as toxic as the full-length protein under conditions where the reception and translocation steps were by-passed. Contrary to the full-length colicin M, the isolated domain did not require the presence of the periplasmic FkpA protein to be toxic under these conditions, demonstrating that FkpA is involved in the maturation process. Mutational analysis further identified five residues that are essential for cytotoxicity as well as in vitro lipid II-degrading activity: Asp-229, His-235, Asp-226, Tyr-228, and Arg-236. Most of these residues are surface-exposed and located relatively close to each other, hence suggesting they belong to the colicin M active site.
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