ArticlePLoS pathogens2016
The Bacterial Flagellar Type III Export Gate Complex Is a Dual Fuel Engine That Can Use Both H+ and Na+ for Flagellar Protein Export.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 79 citations in OpenAlex.
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- RegIIIβ promotes Salmonella Typhimurium colonization of the gut in the early-stage gastrointestinal infection by enhancing flagella-driven locomotion.PLoS pathogens · 2025Article
- A β-cap on the FliPQR protein-export channel acts as the cap for initial flagellar rod assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanisms of antibiofilm compounds JG-1 and M4 across multiple species: alterations of protein interactions essential to biofilm formation.Frontiers in cellular and infection microbiology · 2025Article
- FlaG competes with FliS-flagellin complexes for access to FlhA in the flagellar T3SS to controlProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural basis of directional switching by the bacterial flagellum.Nature microbiology · 2024Article
- FliH and FliI help FlhA bring strict order to flagellar protein export in Salmonella.Communications biology · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Structural Basis of Directional Switching by the Bacterial Flagellum.Research square · 2023Article
- Measurements of the Ion Channel Activity of the Transmembrane Stator Complex in the Bacterial Flagellar Motor.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Purification of the Transmembrane Polypeptide Channel Complex of the Salmonella Flagellar Type III Secretion System.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The Vibrio Polar Flagellum: Structure and Regulation.Advances in experimental medicine and biology · 2023Article
- Conserved GYXLI Motif of FlhA Is Involved in Dynamic Domain Motions of FlhA Required for Flagellar Protein Export.Microbiology spectrum · 2022Article
- Insight Into Distinct Functional Roles of the Flagellar ATPase Complex for Flagellar Assembly inFrontiers in microbiology · 2022Review
- Activation mechanism of the bacterial flagellar dual-fuel protein export engine.Biophysics and physicobiology · 2022Article
- Endophytism: A Multidimensional Approach to Plant-Prokaryotic Microbe Interaction.Frontiers in microbiology · 2022Review
- Structural and Functional Analysis of SsaV Cytoplasmic Domain and Variable Linker States in the Context of the InvA-SsaV Chimeric Protein.Microbiology spectrum · 2021Article
- Membrane voltage-dependent activation mechanism of the bacterial flagellar protein export apparatus.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A positive charge region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export.Communications biology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial flagellar type III export apparatus utilizes ATP and proton motive force (PMF) to transport flagellar proteins to the distal end of the growing flagellar structure for self-assembly. The transmembrane export gate complex is a H+-protein antiporter, of which activity is greatly augmented by an associated cytoplasmic ATPase complex. Here, we report that the export gate complex can use sodium motive force (SMF) in addition to PMF across the cytoplasmic membrane to drive protein export. Protein export was considerably reduced in the absence of the ATPase complex and a pH gradient across the membrane, but Na+ increased it dramatically. Phenamil, a blocker of Na+ translocation, inhibited protein export. Overexpression of FlhA increased the intracellular Na+ concentration in the presence of 100 mM NaCl but not in its absence, suggesting that FlhA acts as a Na+ channel. In wild-type cells, however, neither Na+ nor phenamil affected protein export, indicating that the Na+ channel activity of FlhA is suppressed by the ATPase complex. We propose that the export gate by itself is a dual fuel engine that uses both PMF and SMF for protein export and that the ATPase complex switches this dual fuel engine into a PMF-driven export machinery to become much more robust against environmental changes in external pH and Na+ concentration.
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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.