ArticleScientific reports2018
FliL association with flagellar stator in the sodium-driven Vibrio motor characterized by the fluorescent microscopy.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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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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.
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Who cites it
18 citing papers in PubMed.
- Detection of Ring Structure and Its Flexibility in Periplasmic Region of FliL, Bacterial Flagellar Stator-Associate Protein, in Marine Vibrio.Molecular microbiology · 2026Article
- Signature of cooperativity in the stochastic fluctuations of small systems with application to the bacterial flagellar motor.Scientific reports · 2025Article
- Scrutinizing Stator Rotation in the Bacterial Flagellum: Reconciling Experiments and Switching Models.Biomolecules · 2025Review
- Flagellar motor remodeling during swarming requires FliL.Molecular microbiology · 2023Article
- Flagellar motor remodeling during swarming requires FliL.bioRxiv : the preprint server for biology · 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
- Relaxation time asymmetry in stator dynamics of the bacterial flagellar motor.Science advances · 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 Bacterial Flagellar Motor: Insights Into Torque Generation, Rotational Switching, and Mechanosensing.Frontiers in microbiology · 2022Review
- The Periplasmic Domain of the Ion-Conducting Stator of Bacterial Flagella Regulates Force Generation.Frontiers in microbiology · 2022Review
- Stator Dynamics Depending on Sodium Concentration in Sodium-Driven Bacterial Flagellar Motors.Frontiers in microbiology · 2021Article
- Characterization of FliL Proteins in Bradyrhizobium diazoefficiens: Lateral FliL Supports Swimming Motility, and Subpolar FliL Modulates the Lateral Flagellar System.Journal of bacteriology · 2020Article
- The Three Flagellar Loci ofFrontiers in veterinary science · 2020Article
- New Twists and Turns in Bacterial Locomotion and Signal Transduction.Journal of bacteriology · 2019Review
- Functional Regulators of Bacterial Flagella.Annual review of microbiology · 2019Review
- Structure ofmBio · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Bacterial flagellar motor (BFM) is a protein complex used for bacterial motility and chemotaxis that involves in energy transformation, torque generation and switching. FliL is a single-transmembrane protein associated with flagellar motor function. We performed biochemical and biophysical approaches to investigate the functional roles of FliL associated with stator-units. Firstly, we found the periplasmic region of FliL is crucial for its polar localization. Also, the plug mutation in stator-unit affected the polar localization of FliL implying the activation of stator-unit is important for FliL recruitment. Secondly, we applied single-molecule fluorescent microscopy to study the role of FliL in stator-unit assembly. Using molecular counting by photobleaching, we found the stoichiometry of stator-unit and FliL protein would be 1:1 in a functional motor. Moreover, the turnover time of stator-units are slightly increased in the absence of FliL. By further investigation of protein dynamics on membrane, we found the diffusions of stator-units and FliL are independent. Surprisingly, the FliL diffusion rate without stator-units is unexpectedly slow indicating a protein-complex forming event. Our results suggest that FliL plays a supporting role to the stator in the BFM.
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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.