ArticlePLoS biology2017
A flagellum-specific chaperone facilitates assembly of the core type III export apparatus of the bacterial flagellum.
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 35 papers.
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Who cites it
35 citing papers in PubMed.
- The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026Article
- FliO is an evolutionarily conserved yet diversified core component of the bacterial flagellar type III secretion system.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
- Viscosity-dependent determinants ofmBio · 2024Article
- Genomic diversity of Campylobacter jejuni and Campylobacter coli isolated from the Ethiopian dairy supply chain.PloS one · 2024Article
- Quantifying Substrate Protein Secretion via the Type III Secretion System of the Bacterial Flagellum.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Unrecognized risk of perfluorooctane sulfonate in promoting conjugative transfers of bacterial antibiotic resistance genes.Applied and environmental microbiology · 2023Article
- 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
- Novel transient cytoplasmic rings stabilize assembling bacterial flagellar motors.The EMBO journal · 2022Article
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 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
- Molecular and Cell Biological Analysis of SwrB in Bacillus subtilis.Journal of bacteriology · 2021Article
- Control of membrane barrier during bacterial type-III protein secretion.Nature communications · 2021Article
- A positive charge region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export.Communications biology · 2021Article
- 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
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many bacteria move using a complex, self-assembling nanomachine, the bacterial flagellum. Biosynthesis of the flagellum depends on a flagellar-specific type III secretion system (T3SS), a protein export machine homologous to the export machinery of the virulence-associated injectisome. Six cytoplasmic (FliH/I/J/G/M/N) and seven integral-membrane proteins (FlhA/B FliF/O/P/Q/R) form the flagellar basal body and are involved in the transport of flagellar building blocks across the inner membrane in a proton motive force-dependent manner. However, how the large, multi-component transmembrane export gate complex assembles in a coordinated manner remains enigmatic. Specific for most flagellar T3SSs is the presence of FliO, a small bitopic membrane protein with a large cytoplasmic domain. The function of FliO is unknown, but homologs of FliO are found in >80% of all flagellated bacteria. Here, we demonstrate that FliO protects FliP from proteolytic degradation and promotes the formation of a stable FliP-FliR complex required for the assembly of a functional core export apparatus. We further reveal the subcellular localization of FliO by super-resolution microscopy and show that FliO is not part of the assembled flagellar basal body. In summary, our results suggest that FliO functions as a novel, flagellar T3SS-specific chaperone, which facilitates quality control and productive assembly of the core T3SS export machinery.
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