ArticleNature communications2018
Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026Article
- Active removal of inhibitory components drives the flagellar Type III Secretion Specificity Switch.bioRxiv : the preprint server for biology · 2026Article
- Article
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- Structural basis for substrate specificity switching revealed by the FlhA(A489E) suppressor mutation.Biophysics and physicobiology · 2026Article
- Ultraweak interactions drive cap-mediated positioning and elongation of the bacterial flagellar filament.Nature communications · 2025Article
- Impact of flagellar filament length onJournal of bacteriology · 2025Article
- Bacterial motility depends on a critical flagellum length and energy-optimized assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multiple Chaperone DnaK-FliC Flagellin Interactions are Required for Pseudomonas aeruginosa Flagellum Assembly and Indicate a New Function for DnaK.Microbial biotechnology · 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
- FliH and FliI help FlhA bring strict order to flagellar protein export in Salmonella.Communications biology · 2024Article
- Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone.Protein science : a publication of the Protein Society · 2024Article
- Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica.Nature microbiology · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Back to the Roots:Applied and environmental microbiology · 2023Article
- Advanced liquid crystal-based switchable optical devices for light protection applications: principles and strategies.Light, science & applications · 2023Review
- Molecular Simulation to Investigate Open-Close Motion of a Flagellar Export Apparatus Protein FlhAMethods in molecular biology (Clifton, N.J.) · 2023Article
- Crystals of SctV from different species reveal variable symmetry for the cytosolic domain of the type III secretion system export gate.Acta crystallographica. Section F, Structural biology communications · 2022Article
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Authors and funding
6 authors.
Funding
Abstract
The flagellum and the injectisome enable bacterial locomotion and pathogenesis, respectively. These nanomachines assemble and function using a type III secretion system (T3SS). Exported proteins are delivered to the export apparatus by dedicated cytoplasmic chaperones for their transport through the membrane. The structural and mechanistic basis of this process is poorly understood. Here we report the structures of two ternary complexes among flagellar chaperones (FliT and FliS), protein substrates (the filament-capping FliD and flagellin FliC), and the export gate platform protein FlhA. The substrates do not interact directly with FlhA; however, they are required to induce a binding-competent conformation to the chaperone that exposes the recognition motif featuring a highly conserved sequence recognized by FlhA. The structural data reveal the recognition signal in a class of T3SS proteins and provide new insight into the assembly of key protein complexes at the export gate.
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