ArticleJournal of bacteriology2011
Characterization of the periplasmic region of PomB, a Na+-driven flagellar stator protein in Vibrio alginolyticus.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Cryo-EM structures of the E. coli Ton and Tol motor complexes.Nature communications · 2025Article
- Cryo-EM Structure of the Flagellar Motor Complex fromBiomolecules · 2025Article
- Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS fromBiomolecules · 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
- Ion selectivity and rotor coupling of the Vibrio flagellar sodium-driven stator unit.Nature communications · 2023Article
- Purification of the NaMethods in molecular biology (Clifton, N.J.) · 2023Article
- A new class of biological ion-driven rotary molecular motors with 5:2 symmetry.Frontiers in microbiology · 2022Review
- The Periplasmic Domain of the Ion-Conducting Stator of Bacterial Flagella Regulates Force Generation.Frontiers in microbiology · 2022Review
- Putative Spanner Function of theJournal of bacteriology · 2021Article
- Role of the N- and C-terminal regions of FliF, the MS ring component inJournal of bacteriology · 2021Article
- Essential ion binding residues for NaScientific reports · 2019Article
- Structure ofmBio · 2019Article
- The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum.Journal of bacteriology · 2018Article
- Biochemical analysis of GTPase FlhF which controls the number and position of flagellar formation in marine Vibrio.Scientific reports · 2018Article
- FliL association with flagellar stator in the sodium-driven Vibrio motor characterized by the fluorescent microscopy.Scientific reports · 2018Article
- Functional chimeras of flagellar stator proteins between E. coli MotB and Vibrio PomB at the periplasmic region in Vibrio or E. coli.MicrobiologyOpen · 2015Article
- Serine 26 in the PomB subunit of the flagellar motor is essential for hypermotility of Vibrio cholerae.PloS one · 2015Article
- Interaction of the C-terminal tail of FliF with FliG from the Na+-driven flagellar motor of Vibrio alginolyticus.Journal of bacteriology · 2015Article
- Conformational change in the periplamic region of the flagellar stator coupled with the assembly around the rotor.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The function of the Na+-driven flagellum of Vibrio cholerae is determined by osmolality and pH.Journal of bacteriology · 2013Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The stator proteins PomA and PomB form a complex that couples Na(+) influx to torque generation in the polar flagellar motor of Vibrio alginolyticus. This stator complex is anchored to an appropriate place around the rotor through a putative peptidoglycan-binding (PGB) domain in the periplasmic region of PomB (PomB(C)). To investigate the function of PomB(C), a series of N-terminally-truncated and in-frame mutants with deletions between the transmembrane (TM) segment and the PGB domain of PomB was constructed. A PomB(C) fragment consisting of residues 135 to 315 (PomB(C₅) formed a stable homodimer and significantly inhibited the motility of wild-type cells when overexpressed in the periplasm. A fragment with an in-frame deletion (PomB(ΔL)) of up to 80 residues retained function, and its overexpression with PomA impaired cell growth. This inhibitory effect was suppressed by a mutation at the functionally critical Asp (D24N) in the TM segment of PomB, suggesting that a high level of Na(+) influx through the mutant stator causes the growth impairment. The overproduction of functional PomA/PomB(ΔL) stators also reduced the motile fractions of the cells. That effect could be slightly relieved by a mutation (L168P) in the putative N-terminal α-helix that connects to the PGB domain without affecting the growth inhibition, suggesting that a conformational change of the region including the PGB domain affects stator assembly. Our results reveal common features of the periplasmic region of PomB/MotB and demonstrate that a flexible linker that contains a "plug" segment is important for the control of Na(+) influx through the stator complex as well as for stator assembly.
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