ArticleJournal of bacteriology2010
The flagellar basal body-associated protein FlgT is essential for a novel ring structure in the sodium-driven Vibrio motor.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed.
- Near-atomic in situ architecture and membrane-coupled dynamics of the Vibrio cholerae sheathed flagellum.Nature communications · 2026Article
- Viscosity-dependent determinants ofmBio · 2024Article
- Genomic Analysis of Two Representative Strains ofFoods (Basel, Switzerland) · 2022Article
- Structure and Assembly of the Bacterial Flagellum.Sub-cellular biochemistry · 2022Review
- The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors.Frontiers in microbiology · 2021Review
- The "Jack-of-all-Trades" Flagellum FromFrontiers in microbiology · 2021Article
- Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- The flagellar motor ofeLife · 2020Article
- Living in a Foster Home: The Single Subpolar Flagellum Fla1 ofBiomolecules · 2020Review
- Bacterial flagellar motor PL-ring disassembly subcomplexes are widespread and ancient.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Phylogenetic Distribution, Ultrastructure, and Function of Bacterial Flagellar Sheaths.Biomolecules · 2020Review
- Article
- In situ imaging of the bacterial flagellar motor disassembly and assembly processes.The EMBO journal · 2019Article
- Article
- Characterization of FlgP, an Essential Protein for Flagellar Assembly inJournal of bacteriology · 2019Article
- The presence and absence of periplasmic rings in bacterial flagellar motors correlates with stator type.eLife · 2019Article
- The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum.Journal of bacteriology · 2018Article
- Molecular architecture of the sheathed polar flagellum inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea.Frontiers in microbiology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Vibrio alginolyticus, the flagellar motor can rotate at a remarkably high speed, ca. three to four times faster than the Escherichia coli or Salmonella motor. Here, we found a Vibrio-specific protein, FlgT, in the purified flagellar basal body fraction. Defects of FlgT resulted in partial Fla⁻ and Mot⁻ phenotypes, suggesting that FlgT is involved in formation of the flagellar structure and generating flagellar rotation. Electron microscopic observation of the basal body of ΔflgT cells revealed a smaller LP ring structure compared to the wild type, and most of the T ring was lost. His₆-tagged FlgT could be coisolated with MotY, the T-ring component, suggesting that FlgT may interact with the T ring composed of MotX and MotY. From these lines of evidence, we conclude that FlgT associates with the basal body and is responsible to form an outer ring of the LP ring, named the H ring, which can be distinguished from the LP ring formed by FlgH and FlgI. Vibrio-specific structures, e.g., the T ring and H ring might contribute the more robust motor structure compared to that of E. coli and Salmonella.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.