ArticlePLoS biology2017
Assembly and stoichiometry of the core structure of the bacterial flagellar type III export gate complex.
Article in PLoS biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 79 citations in OpenAlex.
- In vitro biofilm formation by a beneficial bacterium partially predicts in planta protection against rhizosphere pathogens.The ISME journal · 2026Article
- 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
- Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries.Communications biology · 2025Article
- Evaluating the Safety ofMicroorganisms · 2024Article
- Viscosity-dependent determinants ofmBio · 2024Article
- Quantifying Substrate Protein Secretion via the Type III Secretion System of the Bacterial Flagellum.Methods in molecular biology (Clifton, N.J.) · 2024Article
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- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Purification of the Transmembrane Polypeptide Channel Complex of the Salmonella Flagellar Type III Secretion System.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Discovery of a Novel Inner Membrane-Associated Bacterial Structure Related to the Flagellar Type III Secretion System.Journal of bacteriology · 2022Article
- Flagellar energy costs across the tree of life.eLife · 2022Article
- Novel transient cytoplasmic rings stabilize assembling bacterial flagellar motors.The EMBO journal · 2022Article
- Activation mechanism of the bacterial flagellar dual-fuel protein export engine.Biophysics and physicobiology · 2022Article
- Insight Into Distinct Functional Roles of the Flagellar ATPase Complex for Flagellar Assembly inFrontiers in microbiology · 2022Review
- Article
- Article
- Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries.Nature communications · 2021Article
- Control of membrane barrier during bacterial type-III protein secretion.Nature communications · 2021Article
- Molecular structure of the intact bacterial flagellar basal body.Nature microbiology · 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
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial flagellar type III export apparatus, which is required for flagellar assembly beyond the cell membranes, consists of a transmembrane export gate complex and a cytoplasmic ATPase complex. FlhA, FlhB, FliP, FliQ, and FliR form the gate complex inside the basal body MS ring, although FliO is required for efficient export gate formation in Salmonella enterica. However, it remains unknown how they form the gate complex. Here we report that FliP forms a homohexameric ring with a diameter of 10 nm. Alanine substitutions of conserved Phe-137, Phe-150, and Glu-178 residues in the periplasmic domain of FliP (FliPP) inhibited FliP6 ring formation, suppressing flagellar protein export. FliO formed a 5-nm ring structure with 3 clamp-like structures that bind to the FliP6 ring. The crystal structure of FliPP derived from Thermotoga maritia, and structure-based photo-crosslinking experiments revealed that Phe-150 and Ser-156 of FliPP are involved in the FliP-FliP interactions and that Phe-150, Arg-152, Ser-156, and Pro-158 are responsible for the FliP-FliO interactions. Overexpression of FliP restored motility of a ∆fliO mutant to the wild-type level, suggesting that the FliP6 ring is a functional unit in the export gate complex and that FliO is not part of the final gate structure. Copurification assays revealed that FlhA, FlhB, FliQ, and FliR are associated with the FliO/FliP complex. We propose that the assembly of the export gate complex begins with FliP6 ring formation with the help of the FliO scaffold, followed by FliQ, FliR, and FlhB and finally FlhA during MS ring formation.
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