ArticleJournal of bacteriology2014
Contribution of many charged residues at the stator-rotor interface of the Na+-driven flagellar motor to torque generation in Vibrio alginolyticus.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 66 citations in OpenAlex.
- The Regulatory Role of Quorum Sensing-Mediated Amino Acid Metabolism in Biofilm Formation and Motility ofFoods (Basel, Switzerland) · 2026Article
- 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
- Flagellar brake protein YcgR interacts with motor proteins MotA and FliG to regulate the flagellar rotation speed and direction.Frontiers in microbiology · 2023Article
- Ring formation byBiophysics and physicobiology · 2023Article
- Ancestral reconstruction of the MotA stator subunit reveals that conserved residues far from the pore are required to drive flagellar motility.microLife · 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
- Role of the N- and C-terminal regions of FliF, the MS ring component inJournal of bacteriology · 2021Article
- Site-directed crosslinking identifies the stator-rotor interaction surfaces in a hybrid bacterial flagellar motor.Journal of bacteriology · 2021Article
- Construction and Loss of Bacterial Flagellar Filaments.Biomolecules · 2020Review
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- The flagellar motor ofeLife · 2020Article
- Assembly mechanism of a supramolecular MS-ring complex to initiate bacterial flagellar biogenesis inJournal of bacteriology · 2020Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- Evolution of the Stator Elements of Rotary Prokaryote Motors.Journal of bacteriology · 2020Review
- Organization of the Flagellar Switch Complex of Bacillus subtilis.Journal of bacteriology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In torque generation by the bacterial flagellar motor, it has been suggested that electrostatic interactions between charged residues of MotA and FliG at the rotor-stator interface are important. However, the actual role(s) of those charged residues has not yet been clarified. In this study, we systematically made mutants of Vibrio alginolyticus whose charged residues of PomA (MotA homologue) and FliG were replaced by uncharged or charge-reversed residues and characterized the motilities of those mutants. We found that the members of a group of charged residues, 7 in PomA and 6 in FliG, collectively participate in torque generation of the Na(+)-driven flagellar motor in Vibrio. An additional specific interaction between PomA-E97 and FliG-K284 is critical for proper performance of the Vibrio motor. Our results also reveal that more charged residues are involved in the PomA-FliG interactions in the Vibrio Na(+)-driven motor than in the MotA-FliG interactions in the H(+)-driven one. This suggests that a larger number of conserved charged residues at the PomA-FliG interface contributes to the robustness of the Vibrio motor against mutations. The interaction surfaces of the stator and rotor of the Na(+)-driven motor seem to be more complex than those previously proposed in the H(+)-driven motor.
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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.