ReviewJournal of bacteriology2016
ROSET Model of TonB Action in Gram-Negative Bacterial Iron Acquisition.
Review in Journal of bacteriology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 54 citations in OpenAlex.
- Internal Ion Pairs Control Transport Through TonB-Dependent Siderophore Receptors.International journal of molecular sciences · 2026Article
- Revealing Microbial Siderophores: From Genes to Applications.Microorganisms · 2026Review
- New insights into radiolabelled siderophores for molecular imaging of bacterial infections.Npj imaging · 2025Review
- Study in the iron uptake mechanism of Pasteurella multocida.Veterinary research · 2025Review
- The intricacies ofFrontiers in microbiology · 2025Review
- Siderophore-mediated iron acquisition byJournal of bacteriology · 2024Article
- Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu.Frontiers in microbiology · 2024Article
- Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Experimental and computational methods to highlight behavioural variations in TonB-dependent transporter expression in Pseudomonas aeruginosa versus siderophore concentration.Scientific reports · 2023Article
- Iron Acquisition Mechanisms and Their Role in the Virulence of Acinetobacter baumannii.Infection and immunity · 2022Review
- HDX-MS performed on BtuB inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- A new class of biological ion-driven rotary molecular motors with 5:2 symmetry.Frontiers in microbiology · 2022Review
- The Ton Motor.Frontiers in microbiology · 2022Review
- Structural intermediates observed only in intacteLife · 2021Article
- Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics.Chemical reviews · 2021Review
- The Esterase PfeE, the Achilles' Heel in the Battle for Iron betweenInternational journal of molecular sciences · 2021Article
- Genetic and structural determinants on iron assimilation pathways in the plant pathogen Xanthomonas citri subsp. citri and Xanthomonas sp.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Review
- Structure and Stoichiometry of the Ton Molecular Motor.International journal of molecular sciences · 2020Review
- The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model.Nature communications · 2019Article
- Contribution of Active Iron Uptake to Acinetobacter baumannii Pathogenicity.Infection and immunity · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The rotational surveillance and energy transfer (ROSET) model of TonB action suggests a mechanism by which the electrochemical proton gradient across the Gram-negative bacterial inner membrane (IM) promotes the transport of iron through ligand-gated porins (LGP) in the outer membrane (OM). TonB associates with the IM by an N-terminal hydrophobic helix that forms a complex with ExbBD. It also contains a central extended length of rigid polypeptide that spans the periplasm and a dimeric C-terminal-ββαβ-domain (CTD) with LysM motifs that binds the peptidoglycan (PG) layer beneath the OM bilayer. The TonB CTD forms a dimer with affinity for both PG- and TonB-independent OM proteins (e.g., OmpA), localizing it near the periplasmic interface of the OM bilayer. Porins and other OM proteins associate with PG, and this general affinity allows the TonB CTD dimer to survey the periplasmic surface of the OM bilayer. Energized rotational motion of the TonB N terminus in the fluid IM bilayer promotes the lateral movement of the TonB-ExbBD complex in the IM and of the TonB CTD dimer across the inner surface of the OM. When it encounters an accessible TonB box of a (ligand-bound) LGP, the monomeric form of the CTD binds and recruits it into a 4-stranded β-sheet. Because the CTD is rotating, this binding reaction transfers kinetic energy, created by the electrochemical proton gradient across the IM, through the periplasm to the OM protein. The equilibration of the TonB C terminus between the dimeric and monomeric forms that engage in different binding reactions allows the identification of iron-loaded LGP and then the internalization of iron through their trans-outer membrane β-barrels. Hence, the ROSET model postulates a mechanism for the transfer of energy from the IM to the OM, triggering iron uptake.
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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.