ArticleFrontiers in microbiology2016
The FlgT Protein Is Involved in Aeromonas hydrophila Polar Flagella Stability and Not Affects Anchorage of Lateral Flagella.
Article in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Comparative genomics reveals the molecular basis for divergent algicidal strategies in twoApplied and environmental microbiology · 2026Article
- The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026Review
- Ion-Powered Rotary Motors: Where Did They Come from and Where They Are Going?International journal of molecular sciences · 2023Review
- A new class of biological ion-driven rotary molecular motors with 5:2 symmetry.Frontiers in microbiology · 2022Review
- Living in a Foster Home: The Single Subpolar Flagellum Fla1 ofBiomolecules · 2020Review
- Polar Flagella Glycosylation inFrontiers in microbiology · 2020Article
- Comparative Study on A Novel Pathogen of European Seabass. Diversity ofMicroorganisms · 2019Article
- Characterization of FlgP, an Essential Protein for Flagellar Assembly inJournal of bacteriology · 2019Article
- The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum.Journal of bacteriology · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aeromonas hydrophila sodium-driven polar flagellum has a complex stator-motor. Consist of two sets of redundant and non-exchangeable proteins (PomA/PomB and PomA2/PomB2), which are homologs to other sodium-conducting polar flagellum stator motors; and also two essential proteins (MotX and MotY), that they interact with one of those two redundant pairs of proteins and form the T-ring. In this work, we described an essential protein for polar flagellum stability and rotation which is orthologs to Vibrio spp. FlgT and it is encoded outside of the A. hydrophila polar flagellum regions. The flgT was present in all mesophilic Aeromonas strains tested and also in the non-motile Aeromonas salmonicida. The A. hydrophila ΔflgT mutant is able to assemble the polar flagellum but is more unstable and released into the culture supernatant from the cell upon completion assembly. Presence of FlgT in purified polar hook-basal bodies (HBB) of wild-type strain was confirmed by Western blotting and electron microscopy observations showed an outer ring of the T-ring (H-ring) which is not present in the ΔflgT mutant. Anchoring and motility of proton-driven lateral flagella was not affected in the ΔflgT mutant and specific antibodies did not detect FlgT in purified lateral HBB of wild type strain.
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