ArticleMolecular microbiology2013
The unstructured domain of colicin N kills Escherichia coli.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- Modular Platform for Recombinant Production of Highly Toxic Bacterial Proteins.Microbial biotechnology · 2026Article
- The strength of interspecies interaction in a microbial community determines its susceptibility to invasion.PLoS biology · 2024Article
- R-Type Fonticins Produced by Pragia fontium Form Large Pores with High Conductance.Journal of bacteriology · 2023Article
- The evolution of spectrum in antibiotics and bacteriocins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bifurcated binding of the OmpF receptor underpins import of the bacteriocin colicin N intoThe Journal of biological chemistry · 2020Article
- A family of Type VI secretion system effector proteins that form ion-selective pores.Nature communications · 2019Article
- The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Biophysical journal · 2017Article
- A Natural ChimericmBio · 2017Article
- Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA.Microbiology (Reading, England) · 2015Article
- Outer membrane protein F stabilised with minimal amphipol forms linear arrays and LPS-dependent 2D crystals.The Journal of membrane biology · 2014Article
- Daring to be different: colicin N finds another way.Molecular microbiology · 2014Article
- The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein.Molecular microbiology · 2014Article
- Cytotoxic and pathogenic properties of Klebsiella oxytoca isolated from laboratory animals.PloS one · 2014Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Bacteria often produce toxins which kill competing bacteria. Colicins, produced by and toxic to Escherichia coli bacteria are three-domain proteins so efficient that one molecule can kill a cell. The C-terminal domain carries the lethal activity and the central domain is required for surface receptor binding. The N-terminal domain, required for translocation across the outer membrane, is always intrinsically unstructured. It has always been assumed therefore that the C-terminal cytotoxic domain is required for the bactericidal activity. Here we report the unexpected finding that in isolation, the 90-residue unstructured N-terminal domain of colicin N is cytotoxic. Furthermore it causes ion leakage from cells but, unlike known antimicrobial peptides (AMPs) with this property, shows no membrane binding behaviour. Finally, its activity remains strictly dependent upon the same receptor proteins (OmpF and TolA) used by full-length colicin N. This mechanism of rapid membrane disruption, via receptor mediated binding of a soluble peptide, may reveal a new target for the development of highly specific antibacterials.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.