ArticleJournal of bacteriology2006
Roles of charged residues of rotor and stator in flagellar rotation: comparative study using H+-driven and Na+-driven motors in Escherichia coli.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 82 citations in OpenAlex.
- Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS fromBiomolecules · 2025Article
- Regulatory Role of a Hydrophobic Core in the FliG C-Terminal Domain in the Rotary Direction of a Flagellar Motor.Biomolecules · 2025Article
- Structural insight into sodium ion pathway in the bacterial flagellar stator from marineProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Changes in the hydrophobic network of the FliGiScience · 2023Article
- Site-Specific Isotope Labeling of FliG for Studying Structural Dynamics Using Nuclear Magnetic Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Ring formation byBiophysics and physicobiology · 2023Article
- Site-Directed Cross-Linking Between Bacterial Flagellar Motor Proteins In Vivo.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Mutations in the stator protein PomA affect switching of rotational direction in bacterial flagellar motor.Scientific reports · 2022Article
- The Periplasmic Domain of the Ion-Conducting Stator of Bacterial Flagella Regulates Force Generation.Frontiers in microbiology · 2022Review
- Site-directed crosslinking identifies the stator-rotor interaction surfaces in a hybrid bacterial flagellar motor.Journal of bacteriology · 2021Article
- Role of the N- and C-terminal regions of FliF, the MS ring component inJournal of bacteriology · 2021Article
- Structures of the stator complex that drives rotation of the bacterial flagellum.Nature microbiology · 2020Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- The flagellar motor ofeLife · 2020Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- PilG and PilH antagonistically control flagellum-dependent and pili-dependent motility in the phytopathogen Xanthomonas campestris pv. campestris.BMC microbiology · 2020Article
- Organization of the Flagellar Switch Complex of Bacillus subtilis.Journal of bacteriology · 2019Article
- Rotational direction of flagellar motor from the conformation of FliG middle domain in marine Vibrio.Scientific reports · 2018Article
- The role of conserved charged residues in the bidirectional rotation of the bacterial flagellar motor.MicrobiologyOpen · 2018Article
- Pumilacidin-Like Lipopeptides Derived from Marine Bacterium Bacillus sp. Strain 176 Suppress the Motility of Vibrio alginolyticus.Applied and environmental microbiology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
In Escherichia coli, rotation of the flagellar motor has been shown to depend upon electrostatic interactions between charged residues of the stator protein MotA and the rotor protein FliG. These charged residues are conserved in the Na+-driven polar flagellum of Vibrio alginolyticus, but mutational studies in V. alginolyticus suggested that they are relatively unimportant for motor rotation. The electrostatic interactions detected in E. coli therefore might not be a general feature of flagellar motors, or, alternatively, the V. alginolyticus motor might rely on similar interactions but incorporate additional features that make it more robust against mutation. Here, we have carried out a comparative study of chimeric motors that were resident in E. coli but engineered to use V. alginolyticus stator components, rotor components, or both. Charged residues in the V. alginolyticus rotor and stator proteins were found to be essential for motor rotation when the proteins functioned in the setting of the E. coli motor. Patterns of synergism and suppression in rotor/stator double mutants indicate that the V. alginolyticus proteins interact in essentially the same way as their counterparts in E. coli. The robustness of the rotor-stator interface in V. alginolyticus is in part due to the presence of additional charged residues in PomA but appears mainly due to other factors, because an E. coli motor using both rotor and stator components from V. alginolyticus remained sensitive to mutation. Motor function in V. alginolyticus may be enhanced by the proteins MotX and MotY.
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