ArticleMolecular microbiology2010
The colicin Ia receptor, Cir, is also the translocator for colicin Ia.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 59 citations in OpenAlex.
- Bacterial weaponry and the ecological factors of competitive success.Essays in biochemistry · 2026Review
- Salt bridge disruption in colicin Ib channel-forming domain enhances membrane translocation and bactericidal activity.Journal of structural biology: X · 2026Article
- Structural insights into Cir-mediated killing by the antimicrobial protein Microcin V.Communications biology · 2025Article
- Article
- The Biology of Colicin M and Its Orthologs.Antibiotics (Basel, Switzerland) · 2021Review
- An Update on Wastewater Multi-Resistant Bacteria: Identification of Clinical Pathogens Such asMicroorganisms · 2021Article
- Targeted Delivery of Narrow-Spectrum Protein Antibiotics to the Lower Gastrointestinal Tract in a Murine Model ofFrontiers in microbiology · 2021Article
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- A membrane-depolarizing toxin substrate of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Optimizing Cell-Free Protein Synthesis for Increased Yield and Activity of Colicins.Methods and protocols · 2019Article
- Tools and Approaches for Dissecting Protein Bacteriocin Import in Gram-Negative Bacteria.Frontiers in microbiology · 2019Review
- Rapid production and characterization of antimicrobial colicins usingSynthetic biology (Oxford, England) · 2018Article
- The Colicin E1 TolC Box: Identification of a Domain Required for Colicin E1 Cytotoxicity and TolC Binding.Journal of bacteriology · 2017Article
- Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa.The Biochemical journal · 2016Article
- From Homodimer to Heterodimer and Back: Elucidating the TonB Energy Transduction Cycle.Journal of bacteriology · 2015Article
- The proton-motive force is required for translocation of CDI toxins across the inner membrane of target bacteria.Molecular microbiology · 2014Article
- Regulatory RNAs involved in bacterial antibiotic resistance.PLoS pathogens · 2014Review
- Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake.Molecular microbiology · 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
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2 authors at 1 institution in 1 country.
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Abstract
Colicin Ia, a channel-forming bactericidal protein, uses the outer membrane protein, Cir, as its primary receptor. To kill Escherichia coli, it must cross this membrane. The crystal structure of Ia receptor-binding domain bound to Cir, a 22-stranded plugged beta-barrel protein, suggests that the plug does not move. Therefore, another pathway is needed for the colicin to cross the outer membrane, but no 'second receptor' has ever been identified for TonB-dependent colicins, such as Ia. We show that if the receptor-binding domain of colicin Ia is replaced by that of colicin E3, this chimera effectively kills cells, provided they have the E3 receptor (BtuB), Cir, and TonB. This is consistent with wild-type Ia using one Cir as its primary receptor (BtuB in the chimera) and a second Cir as the translocation pathway for its N-terminal translocation (T) domain and its channel-forming C-terminal domain. Deletion of colicin Ia's receptor-binding domain results in a protein that kills E. coli, albeit less effectively, provided they have Cir and TonB. We show that purified T domain competes with Ia and protects E. coli from being killed by it. Thus, in addition to binding to colicin Ia's receptor-binding domain, Cir also binds weakly to its translocation domain.
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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.