ArticleJournal of bacteriology2010
The flagellar protein FliL is essential for swimming in Rhodobacter sphaeroides.
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 38 papers.
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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.
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Who cites it
38 citing papers in PubMed, 50 citations in OpenAlex.
- Detection of Ring Structure and Its Flexibility in Periplasmic Region of FliL, Bacterial Flagellar Stator-Associate Protein, in Marine Vibrio.Molecular microbiology · 2026Article
- Flagellar protein FliL: A many-splendored thing.Molecular microbiology · 2024Review
- VirB11, a traffic ATPase, mediated flagella assembly and type IV pilus morphogenesis to control the motility and virulence of Xanthomonas albilineans.Molecular plant pathology · 2024Article
- Article
- Flagellar motor remodeling during swarming requires FliL.Molecular microbiology · 2023Article
- Molecular characterization and in-depth genome analysis of Enterobacter sp. S-16.Functional & integrative genomics · 2023Article
- Flagellar motor remodeling during swarming requires FliL.bioRxiv : the preprint server for biology · 2023Article
- FliL Functions in Diverse Microbes to Negatively Modulate Motor Output via Its N-Terminal Region.mBio · 2023Article
- FlgV forms a flagellar motor ring that is required for optimal motility of Helicobacter pylori.PloS one · 2023Article
- FliL Differentially Interacts with Two Stator Systems To Regulate Flagellar Motor Output in Pseudomonas aeruginosa.Applied and environmental microbiology · 2022Article
- FliL and its paralog MotF have distinct roles in the stator activity of the Sinorhizobium meliloti flagellar motor.Molecular microbiology · 2022Article
- FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Surveying a Swarm: Experimental Techniques To Establish and Examine Bacterial Collective Motion.Applied and environmental microbiology · 2022Article
- The flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Periplasmic Domain of the Ion-Conducting Stator of Bacterial Flagella Regulates Force Generation.Frontiers in microbiology · 2022Review
- Swimming Using a Unidirectionally Rotating, Single Stopping Flagellum in the Alpha ProteobacteriumFrontiers in microbiology · 2022Review
- Living in a Foster Home: The Single Subpolar Flagellum Fla1 ofBiomolecules · 2020Review
- Functional Regulators of Bacterial Flagella.Annual review of microbiology · 2019Review
- Structure ofmBio · 2019Article
- A tetratricopeptide repeat domain protein has profound effects on assembly of periplasmic flagella, morphology and motility of the lyme disease spirochete Borrelia burgdorferi.Molecular microbiology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this work we characterize the function of the flagellar protein FliL in Rhodobacter sphaeroides. Our results show that FliL is essential for motility in this bacterium and that in its absence flagellar rotation is highly impaired. A green fluorescent protein (GFP)-FliL fusion forms polar and lateral fluorescent foci that show different spatial dynamics. The presence of these foci is dependent on the expression of the flagellar genes controlled by the master regulator FleQ, suggesting that additional components of the flagellar regulon are required for the proper localization of GFP-FliL. Eight independent pseudorevertants were isolated from the fliL mutant strain. In each of these strains a single nucleotide change in motB was identified. The eight mutations affected only three residues located on the periplasmic side of MotB. Swimming of the suppressor mutants was not affected by the presence of the wild-type fliL allele. Pulldown and yeast two-hybrid assays showed that that the periplasmic domain of FliL is able to interact with itself but not with the periplasmic domain of MotB. From these results we propose that FliL could participate in the coupling of MotB with the flagellar rotor in an indirect fashion.
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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.