ArticleJournal of bacteriology2008
Characterization of the periplasmic domain of MotB and implications for its role in the stator assembly of the bacterial flagellar motor.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Impact of flagellar filament length onJournal of bacteriology · 2025Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Measurements of the Ion Channel Activity of the Transmembrane Stator Complex in the Bacterial Flagellar Motor.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Dynamics of the Two Stator Systems in the Flagellar Motor of Pseudomonas aeruginosa Studied by a Bead Assay.Applied and environmental microbiology · 2021Article
- Architecture and Assembly of the Bacterial Flagellar Motor Complex.Sub-cellular biochemistry · 2021Review
- GFP Fusion to the N-Terminus of MotB Affects the Proton Channel Activity of the Bacterial Flagellar Motor inBiomolecules · 2020Article
- Understanding and Exploiting Phage-Host Interactions.Viruses · 2019Review
- Evidence for the hook supercoiling mechanism of the bacterial flagellum.Biophysics and physicobiology · 2018Article
- Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper.Scientific reports · 2017Article
- Load- and polysaccharide-dependent activation of the NaScientific reports · 2017Article
- Structure and function of the bi-directional bacterial flagellar motor.Biomolecules · 2014Review
- Effect of the MotB(D33N) mutation on stator assembly and rotation of the proton-driven bacterial flagellar motor.Biophysics (Nagoya-shi, Japan) · 2014Article
- The C-terminal periplasmic domain of MotB is responsible for load-dependent control of the number of stators of the bacterial flagellar motor.Biophysics (Nagoya-shi, Japan) · 2013Article
- Intragenic suppressor of a plug deletion nonmotility mutation in PotB, a chimeric stator protein of sodium-driven flagella.Journal of bacteriology · 2012Article
- Characterization of the periplasmic region of PomB, a Na+-driven flagellar stator protein in Vibrio alginolyticus.Journal of bacteriology · 2011Article
- Structure of the flagellar motor protein complex PomAB: implications for the torque-generating conformation.Journal of bacteriology · 2011Article
- Development of real-time PCR assays for detection and quantification of Bacillus cereus group species: differentiation of B. weihenstephanensis and rhizoid B. pseudomycoides isolates from milk.Applied and environmental microbiology · 2011Article
- Bacterial nanomachines: the flagellum and type III injectisome.Cold Spring Harbor perspectives in biology · 2010Review
- Isolation of basal bodies with C-ring components from the Na+-driven flagellar motor of Vibrio alginolyticus.Journal of bacteriology · 2010Article
- Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: implications for peptidoglycan recognition.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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5 authors.
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Abstract
MotA and MotB are integral membrane proteins that form the stator complex of the proton-driven bacterial flagellar motor. The stator complex functions as a proton channel and couples proton flow with torque generation. The stator must be anchored to an appropriate place on the motor, and this is believed to occur through a putative peptidoglycan-binding (PGB) motif within the C-terminal periplasmic domain of MotB. In this study, we constructed and characterized an N-terminally truncated variant of Salmonella enterica serovar Typhimurium MotB consisting of residues 78 through 309 (MotB(C)). MotB(C) significantly inhibited the motility of wild-type cells when exported into the periplasm. Some point mutations in the PGB motif enhanced the motility inhibition, while an in-frame deletion variant, MotB(C)(Delta197-210), showed a significantly reduced inhibitory effect. Wild-type MotB(C) and its point mutant variants formed a stable homodimer, while the deletion variant was monomeric. A small amount of MotB was coisolated only with the secreted form of MotB(C)-His(6) by Ni-nitrilotriacetic acid affinity chromatography, suggesting that the motility inhibition results from MotB-MotB(C) heterodimer formation in the periplasm. However, the monomeric mutant variant MotB(C)(Delta197-210) did not bind to MotB, suggesting that MotB(C) is directly involved in stator assembly. We propose that the MotB(C) dimer domain plays an important role in targeting and stable anchoring of the MotA/MotB complex to putative stator-binding sites of the motor.
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