ArticleProceedings of the National Academy of Sciences of the United States of America2005
Cell entry mechanism of enzymatic bacterial colicins: porin recruitment and the thermodynamics of receptor binding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 94 citations in OpenAlex.
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Antimicrobial Peptides (Bacteriocins) Produced by Lactococcus lactis and Pediococcus pentosaceus Strains with Activity Against Clinical and Food-Borne Pathogens.Probiotics and antimicrobial proteins · 2025Article
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- Structural constraints of pyocin S2 import through the ferripyoverdine receptor FpvAI.PNAS nexus · 2024Article
- Conformational rearrangements in the sensory RcsF/OMP complex mediate signal transduction across the bacterial cell envelope.PLoS genetics · 2023Article
- Lipids mediate supramolecular outer membrane protein assembly in bacteria.Science advances · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Colicin E1 opens its hinge to plug TolC.eLife · 2022Article
- Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.The EMBO journal · 2021Article
- COVID-19: insights into virus-receptor interactions.Molecular biomedicine · 2021Article
- Bacterial Vivisection: How Fluorescence-Based Imaging Techniques Shed a Light on the Inner Workings of Bacteria.Microbiology and molecular biology reviews : MMBR · 2020Review
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- Transmembrane Epitope Delivery by Passive Protein Threading through the Pores of the OmpF Porin Trimer.Journal of the American Chemical Society · 2020Article
- Targeted Killing of Pseudomonas aeruginosa by Pyocin G Occurs via the Hemin Transporter Hur.Journal of molecular biology · 2020Article
- Pyocin S5 Import into Pseudomonas aeruginosa Reveals a Generic Mode of Bacteriocin Transport.mBio · 2020Article
- O-Antigen-Dependent Colicin Insensitivity of Uropathogenic Escherichia coli.Journal of bacteriology · 2019Article
- Tools and Approaches for Dissecting Protein Bacteriocin Import in Gram-Negative Bacteria.Frontiers in microbiology · 2019Review
- Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.EcoSal Plus · 2019Review
- Development of a biosensor protein bullet as a fluorescent method for fast detection of Escherichia coli in drinking water.PloS one · 2018Article
- The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Biophysical journal · 2017Article
1 more citing papers are in PubMed but not listed here.
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5 authors at 3 institutions in 1 country.
Funding
Abstract
Binding of enzymatic E colicins to the vitamin B12 receptor, BtuB, is the first stage in a cascade of events that culminate in the translocation of the cytotoxic nuclease into the Escherichia coli cytoplasm and release of its tightly bound immunity protein. A dogma of colicin biology is that the toxin coiled-coil connecting its functional domains must unfold or unfurl to span the periplasm, with recent reports claiming this reaction is initiated by receptor binding. We report isothermal titration calorimetry data of BtuB binding the endonuclease toxin ColE9 and a disulfide form (ColE9S-S) where unfolding of the coiled-coil is prevented and, as a consequence, the toxin is biologically inactive. Contrary to expectation, the thermodynamics of receptor binding, characterized by large negative values for TDeltaS, are identical for the two colicins, arguing against any form of BtuB-induced unfolding. We go on to delineate key features of the "colicin translocon" that assembles at the cell surface after BtuB binding by using a complex of histidine-tagged Im9 bound to ColE9S-S. First, we show that the porin OmpF is recruited directly to the BtuB.colicin complex to form the translocon. Second, recruitment is through the natively unfolded region of the colicin translocation domain, with this domain likely having two contact points for OmpF. Finally, the immunity protein is not released during its assembly. Our study demonstrates that although colicin unfolding is undoubtedly a prerequisite for E. coli cell death, it must occur after assembly of the translocon.
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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.