ArticleMolecular microbiology2009
Fluoresceination of FepA during colicin B killing: effects of temperature, toxin and TonB.
Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Internal Ion Pairs Control Transport Through TonB-Dependent Siderophore Receptors.International journal of molecular sciences · 2026Article
- Siderophore-mediated iron acquisition byJournal of bacteriology · 2024Article
- Fluorescent Binding Protein Sensors for Detection and Quantification of Biochemicals, Metabolites, and Natural Products.Bio-protocol · 2022Article
- Article
- Conformational rearrangements in the N-domain ofThe Journal of biological chemistry · 2020Article
- Fluorescence High-Throughput Screening for Inhibitors of TonB Action.Journal of bacteriology · 2017Article
- Going Outside the TonB Box: Identification of Novel FepA-TonB InteractionsJournal of bacteriology · 2017Article
- Article
- The proton-motive force is required for translocation of CDI toxins across the inner membrane of target bacteria.Molecular microbiology · 2014Article
- Concerted loop motion triggers induced fit of FepA to ferric enterobactin.The Journal of general physiology · 2014Article
- Energy-dependent motion of TonB in the Gram-negative bacterial inner membrane.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Use of a molecular decoy to segregate transport from antigenicity in the FrpB iron transporter from Neisseria meningitidis.PloS one · 2013Article
- Direct measurements of the outer membrane stage of ferric enterobactin transport: postuptake binding.The Journal of biological chemistry · 2010Article
- The colicin Ia receptor, Cir, is also the translocator for colicin Ia.Molecular microbiology · 2010Article
- TonB-dependent transporters: regulation, structure, and function.Annual review of microbiology · 2010Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We studied the reactivity of 35 genetically engineered Cys sulphydryl groups at different locations in Escherichia coli FepA. Modification of surface loop residues by fluorescein maleimide (FM) was strongly temperature-dependent in vivo, whereas reactivity at other sites was much less affected. Control reactions with bovine serum albumin showed that the temperature dependence of loop residue reactivity was unusually high, indicating that conformational changes in multiple loops (L2, L3, L4, L5, L7, L8, L10) transform the receptor to a more accessible form at 37 degrees C. At 0 degrees C colicin B binding impaired or blocked labelling at 8 of 10 surface loop sites, presumably by steric hindrance. Overall, colicin B adsorption decreased the reactivity of more than half of the 35 sites, in both the N- and C- domains of FepA. However, colicin B penetration into the cell at 37 degrees C did not augment the chemical modification of any residues in FepA. The FM modification patterns were similarly unaffected by the tonB locus. FepA was expressed at lower levels in a tonB host strain, but when we accounted for this decrease its FM labelling was comparable whether TonB was present or absent. Thus we did not detect TonB-dependent structural changes in FepA, either alone or when it interacted with colicin B at 37 degrees C. The only changes in chemical modification were reductions from steric hindrance when the bacteriocin bound to the receptor protein. The absence of increases in the reactivity of N-domain residues argues against the idea that the colicin B polypeptide traverses the FepA channel.
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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.