ArticleThe Journal of biological chemistry2012
Functional and structural characterization of PaeM, a colicin M-like bacteriocin produced by Pseudomonas aeruginosa.
Article in The Journal of biological chemistry, 2012. 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, 61 citations in OpenAlex.
- Article
- 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
- Cytotoxic rhamnolipid micelles drive acute virulence inInfection and immunity · 2024Article
- Biosynthetic gene cluster signature profiles of pathogenic Gram-negative bacteria isolated from Egyptian clinical settings.Microbiology spectrum · 2023Article
- Outer membrane translocation of pyocins via the copper regulated TonB-dependent transporter CrtA.The Biochemical journal · 2023Article
- Metagenome-mining indicates an association between bacteriocin presence and strain diversity in the infant gut.BMC genomics · 2023Article
- MvaT negatively regulates pyocin S5 expression inBiotechnology notes (Amsterdam, Netherlands) · 2022Article
- The Biology of Colicin M and Its Orthologs.Antibiotics (Basel, Switzerland) · 2021Review
- Pyocin S5 Import into Pseudomonas aeruginosa Reveals a Generic Mode of Bacteriocin Transport.mBio · 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
- Article
- A Natural ChimericmBio · 2017Article
- Novel Immunity Proteins Associated with Colicin M-like Bacteriocins Exhibit Promiscuous Protection inFrontiers in microbiology · 2017Article
- Article
- Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression.Antibiotics (Basel, Switzerland) · 2016Article
- Structural and biophysical analysis of nuclease protein antibiotics.The Biochemical journal · 2016Article
- Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa.The Biochemical journal · 2016Article
- Efficacy of species-specific protein antibiotics in a murine model of acute Pseudomonas aeruginosa lung infection.Scientific reports · 2016Article
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Authors and funding
13 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Colicin M (ColM) is the only enzymatic colicin reported to date that inhibits cell wall peptidoglycan biosynthesis. It catalyzes the specific degradation of the lipid intermediates involved in this pathway, thereby provoking lysis of susceptible Escherichia coli cells. A gene encoding a homologue of ColM was detected within the exoU-containing genomic island A carried by certain pathogenic Pseudomonas aeruginosa strains. This bacteriocin (pyocin) that we have named PaeM was crystallized, and its structure with and without an Mg(2+) ion bound was solved. In parallel, site-directed mutagenesis of conserved PaeM residues from the C-terminal domain was performed, confirming their essentiality for the protein activity both in vitro (lipid II-degrading activity) and in vivo (cytotoxicity against a susceptible P. aeruginosa strain). Although PaeM is structurally similar to ColM, the conformation of their active sites differs radically; in PaeM, residues essential for enzymatic activity and cytotoxicity converge toward a same pocket, whereas in ColM they are spread along a particularly elongated active site. We have also isolated a minimal domain corresponding to the C-terminal half of the PaeM protein and exhibiting a 70-fold higher enzymatic activity as compared with the full-length protein. This isolated domain of the PaeM bacteriocin was further shown to kill E. coli cells when addressed to the periplasm of these bacteria.
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