ArticleJournal of bacteriology2001
Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 64 citations in OpenAlex.
- The structures and functions of Salmonella outer membrane.Archives of microbiology · 2026Review
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- A TrmBL2-like transcription factor mediates the growth phase-dependent expression of halolysin SptA in a concentration-dependent manner inApplied and environmental microbiology · 2024Article
- Auto- and Hetero-Catalytic Processing of the N-Terminal Propeptide Promotes the C-Terminal Fibronectin Type III Domain-Mediated Dimerization of a Thermostable Vpr-like Protease.Applied and environmental microbiology · 2022Article
- Extraintestinal PathogenicMicrobiology spectrum · 2022Article
- A Dynamic Protein-Protein Coupling between the TonB-Dependent Transporter FhuA and TonB.Biochemistry · 2018Article
- Membrane Protein Complex ExbB4-ExbD1-TonB1 from Escherichia coli Demonstrates Conformational Plasticity.Journal of bacteriology · 2015Article
- Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex.Biochemistry · 2013Article
- The Vibrio cholerae VctPDGC system transports catechol siderophores and a siderophore-free iron ligand.Molecular microbiology · 2011Article
- Bacterial heme-transport proteins and their heme-coordination modes.Archives of biochemistry and biophysics · 2009Review
- 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
- Signaling mechanisms for activation of extracytoplasmic function (ECF) sigma factors.Biochimica et biophysica acta · 2008Review
- Interaction of TonB with the outer membrane receptor FpvA of Pseudomonas aeruginosa.Journal of bacteriology · 2006Article
- Crystallization and preliminary X-ray crystallographic analysis of the Escherichia coli outer membrane cobalamin transporter BtuB in complex with the carboxy-terminal domain of TonB.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Import of the transfer RNase colicin D requires site-specific interaction with the energy-transducing protein TonB.Journal of bacteriology · 2005Article
- In vivo evidence for TonB dimerization.Journal of bacteriology · 2003Article
- Differential substrate-induced signaling through the TonB-dependent transporter BtuB.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box.Journal of bacteriology · 2003Article
- Demonstration and characterization of a specific interaction between gonococcal transferrin binding protein A and TonB.Journal of bacteriology · 2002Article
- Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein.The EMBO journal · 2002Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High-affinity iron uptake in gram-negative bacteria depends upon TonB, a protein which couples the proton motive force in the cytoplasmic membrane to iron chelate receptors in the outer membrane. To advance studies on TonB structure and function, we expressed a recombinant form of Escherichia coli TonB lacking the N-terminal cytoplasmic membrane anchor. This protein (H(6)-'TonB; M(r), 24,880) was isolated in a soluble fraction of lysed cells and was purified by virtue of a hexahistidine tag located at its N terminus. Sedimentation experiments indicated that the H(6)-'TonB preparation was almost monodisperse and the protein was essentially monomeric. The value found for the Stokes radius (3.8 nm) is in good agreement with the value calculated by size exclusion chromatography. The frictional ratio (2.0) suggested that H(6)-'TonB adopts a highly asymmetrical form with an axial ratio of 15. H(6)-'TonB captured both the ferrichrome-iron receptor FhuA and the ferric enterobactin receptor FepA from detergent-solubilized outer membranes in vitro. Capture was enhanced by preincubation of the receptors with their cognate ligands. Cross-linking assays with the purified proteins in vitro demonstrated that there was preferential interaction between TonB and ligand-loaded FhuA. Purified H(6)-'TonB was found to be stable and thus shows promise for high-resolution structural studies.
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