ArticleJournal of bacteriology2001
In vivo synthesis of the periplasmic domain of TonB inhibits transport through the FecA and FhuA iron siderophore transporters of Escherichia coli.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Prevalence of bovine endometritis, virulence mechanisms ofVirulence · 2026Pooled it
- Study of excess manganese stress response highlights the central role of manganese exporter Mnx for holding manganese homeostasis in the cyanobacteriumMicrobiology (Reading, England) · 2024Article
- Siderophores: A Case Study in Translational Chemical Biology.Biochemistry · 2024Review
- Trojan Horse Siderophore Conjugates InduceJournal of medicinal chemistry · 2023Article
- Hybrid Vigor: Importance of Hybrid λ Phages in Early Insights in Molecular Biology.Microbiology and molecular biology reviews : MMBR · 2022Review
- The evolution of coexistence from competition in experimental co-cultures of Escherichia coli and Saccharomyces cerevisiae.The ISME journal · 2021Article
- Bacterial iron acquisition mediated by outer membrane translocation and cleavage of a host protein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Interaction of the colicin K bactericidal toxin with components of its import machinery in the periplasm of Escherichia coli.Journal of bacteriology · 2010Article
- TonB induces conformational changes in surface-exposed loops of FhuA, outer membrane receptor of Escherichia coli.Protein science : a publication of the Protein Society · 2008Article
- Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane.Journal of bacteriology · 2008Article
- Deletion and substitution analysis of the Escherichia coli TonB Q160 region.Journal of bacteriology · 2007Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- Interaction of TonB with the outer membrane receptor FpvA of Pseudomonas aeruginosa.Journal of bacteriology · 2006Article
- In vivo evidence for TonB dimerization.Journal of bacteriology · 2003Article
- In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12.Journal of bacteriology · 2003Article
- Performance of standard phenotypic assays for TonB activity, as evaluated by varying the level of functional, wild-type TonB.Journal of bacteriology · 2003Article
- Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box.Journal of bacteriology · 2003Article
- Analysis of residues determining specificity of Vibrio cholerae TonB1 for its receptors.Journal of bacteriology · 2003Article
- Mutational analysis of the TonB1 energy coupler of Pseudomonas aeruginosa.Journal of bacteriology · 2002Article
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4 authors.
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Abstract
The siderophore transport activities of the two outer membrane proteins FhuA and FecA of Escherichia coli require the proton motive force of the cytoplasmic membrane. The energy of the proton motive force is postulated to be transduced to the transport proteins by a protein complex that consists of the TonB, ExbB, and ExbD proteins. In the present study, TonB fragments lacking the cytoplasmic membrane anchor were exported to the periplasm by fusing them to the cleavable signal sequence of FecA. Overexpressed TonB(33-239), TonB(103-239), and TonB(122-239) fragments inhibited transport of ferrichrome by FhuA and of ferric citrate by FecA, transcriptional induction of the fecABCDE transport genes by FecA, infection by phage phi80, and killing of cells by colicin M via FhuA. Transport of ferrichrome by FhuADelta5-160 was also inhibited by TonB(33-239), although FhuADelta5-160 lacks the TonB box which is involved in TonB binding. The results show that TonB fragments as small as the last 118 amino acids of the protein interfere with the function of wild-type TonB, presumably by competing for binding sites at the transporters or by forming mixed dimers with TonB that are nonfunctional. In addition, the interactions that are inhibited by the TonB fragments must include more than the TonB box, since transport through corkless FhuA was also inhibited. Since the periplasmic TonB fragments cannot assume an energized conformation, these in vivo studies also agree with previous cross-linking and in vitro results, suggesting that neither recognition nor binding to loaded siderophore receptors is the energy-requiring step in the TonB-receptor interactions.
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