ArticleProceedings of the National Academy of Sciences of the United States of America2016
Recognition and targeting mechanisms by chaperones in flagellum assembly and operation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Active removal of inhibitory components drives the flagellar type 3 secretion-specificity switch.mBio · 2026Article
- Active removal of inhibitory components drives the flagellar Type III Secretion Specificity Switch.bioRxiv : the preprint server for biology · 2026Article
- Remote on-off switching of protein activity by intrinsically disordered region.Nature structural & molecular biology · 2025Article
- Impact of flagellar filament length onJournal of bacteriology · 2025Article
- The Flagellin-Specific Chaperone FliS of Borrelia burgdorferi Controls the Cytoplasmic Pool of Flagellins at the Level of Translation Initiation, Secretion, and Proteolysis.Molecular 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 for the dynamic chaperoning of disordered clients by Hsp90.Nature structural & molecular 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
- Genome-wide analysis reveals a rhamnolipid-dependent modulation of flagellar genes in Pseudomonas aeruginosa PAO1.Current genetics · 2022Article
- Performance of halotolerant bacteria associated with Sahara-inhabiting halophytes Atriplex halimus L. and Lygeum spartum L. ameliorate tomato plant growth and tolerance to saline stress: from selective isolation to genomic analysis of potential determinants.World journal of microbiology & biotechnology · 2021Article
- Molecular Determinants of Filament Capping Proteins Required for the Formation of Functional Flagella in Gram-Negative Bacteria.Biomolecules · 2021Article
- Bacterial Flagellar Filament: A Supramolecular Multifunctional Nanostructure.International journal of molecular sciences · 2021Review
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- Multiple Roles of Flagellar Export Chaperones for Efficient and Robust Flagellar Filament Formation inFrontiers in microbiology · 2021Article
- Structural basis for client recognition and activity of Hsp40 chaperones.Science (New York, N.Y.) · 2019Article
- Structural Basis for the Inhibition of the Autophosphorylation Activity of HK853 by Luteolin.Molecules (Basel, Switzerland) · 2019Article
- Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system.Nature communications · 2018Article
- RpoN2- and FliA-regulated fliTX is indispensible for flagellar motility and virulence in Xanthomonas oryzae pv. oryzae.BMC microbiology · 2017Article
- The role of the FliD C-terminal domain in pentamer formation and interaction with FliT.Scientific reports · 2017Article
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4 authors.
Funding
Abstract
The flagellum is a complex bacterial nanomachine that requires the proper assembly of several different proteins for its function. Dedicated chaperones are central in preventing aggregation or undesired interactions of flagellar proteins, including their targeting to the export gate. FliT is a key flagellar chaperone that binds to several flagellar proteins in the cytoplasm, including its cognate filament-capping protein FliD. We have determined the solution structure of the FliT chaperone in the free state and in complex with FliD and the flagellar ATPase FliI. FliT adopts a four-helix bundle and uses a hydrophobic surface formed by the first three helices to recognize its substrate proteins. We show that the fourth helix constitutes the binding site for FlhA, a membrane protein at the export gate. In the absence of a substrate protein FliT adopts an autoinhibited structure wherein both the binding sites for substrates and FlhA are occluded. Substrate binding to FliT activates the complex for FlhA binding and thus targeting of the chaperone-substrate complex to the export gate. The activation and targeting mechanisms reported for FliT appear to be shared among the other flagellar chaperones.
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