ArticleScientific reports2014
Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 78 citations in OpenAlex.
- Article
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- On the role of the sorting platform in hierarchical type III secretion regulation in enteropathogenicJournal of bacteriology · 2025Article
- Mapping the loss of flagellar motility across the tree of life.The ISME journal · 2025Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- 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
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Distinct Cytosolic Complexes Containing the Type III Secretion System ATPase Resolved by Three-Dimensional Single-Molecule Tracking in Live Yersinia enterocolitica.Microbiology spectrum · 2022Article
- Endophytism: A Multidimensional Approach to Plant-Prokaryotic Microbe Interaction.Frontiers in microbiology · 2022Review
- 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
- A positive charge region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export.Communications biology · 2021Article
- Review
- Protein Export via the Type III Secretion System of the Bacterial Flagellum.Biomolecules · 2021Review
- Architecture and Assembly of the Bacterial Flagellar Motor Complex.Sub-cellular biochemistry · 2021Review
- Construction and Loss of Bacterial Flagellar Filaments.Biomolecules · 2020Review
- FliIScientific reports · 2020Article
- Flagella-Driven Motility of Bacteria.Biomolecules · 2019Review
- Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.Nature communications · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For construction of the bacterial flagellum, FliI ATPase forms the FliH2-FliI complex in the cytoplasm and localizes to the flagellar basal body (FBB) through the interaction of FliH with a C ring protein, FliN. FliI also assembles into a homo-hexamer to promote initial entry of export substrates into the export gate. The interaction of FliH with an export gate protein, FlhA, is required for stable anchoring of the FliI6 ring to the gate. Here we report the stoichiometry and assembly dynamics of FliI-YFP by fluorescence microscopy with single molecule precision. More than six FliI-YFP molecules were associated with the FBB through interactions of FliH with FliN and FlhA. Single FliI-YFP molecule exchanges between the FBB-localized and free-diffusing ones were observed several times per minute. Neither the number of FliI-YFP associated with the FBB nor FliI-YFP turnover rate were affected by catalytic mutations in FliI, indicating that ATP hydrolysis by FliI does not drive the assembly-disassembly cycle of FliI during flagellar assembly. We propose that the FliH2FliI complex and FliI6 ring function as a dynamic substrate carrier and a static substrate loader, respectively.
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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.