ArticleBiophysics (Nagoya-shi, Japan)2013
The C-terminal periplasmic domain of MotB is responsible for load-dependent control of the number of stators of the bacterial flagellar motor.
Article in Biophysics (Nagoya-shi, Japan), 2013. 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.
- Signature of cooperativity in the stochastic fluctuations of small systems with application to the bacterial flagellar motor.Scientific reports · 2025Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- A bacterial sense of touch: T4P retraction motor as a means of surface sensing byJournal of bacteriology · 2024Review
- Viscosity-dependent determinants ofmBio · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Relaxation time asymmetry in stator dynamics of the bacterial flagellar motor.Science advances · 2022Article
- Mechanosensitive recruitment of stator units promotes binding of the response regulator CheY-P to the flagellar motor.Nature communications · 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
- Spirochete Flagella and Motility.Biomolecules · 2020Review
- Dynamic exchange of two types of stator units inComputational and structural biotechnology journal · 2020Review
- Article
- Flagella-Driven Motility of Bacteria.Biomolecules · 2019Review
- Evaluation of the Duty Ratio of the Bacterial Flagellar Motor by Dynamic Load Control.Biophysical journal · 2019Article
- Salmonella Typhimurium is Attracted to Egg Yolk and Repelled by Albumen.Current microbiology · 2019Article
- Structure ofmBio · 2019Article
- Effect of the MotA(M206I) Mutation on Torque Generation and Stator Assembly in theJournal of bacteriology · 2019Article
- NaScience advances · 2017Article
- Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper.Scientific reports · 2017Article
- Torque, but not FliL, regulates mechanosensitive flagellar motor-function.Scientific reports · 2017Article
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8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial flagellar motor is made of a rotor and stators. In Salmonella it is thought that about a dozen MotA/B complexes are anchored to the peptidoglycan layer around the motor through the C-terminal peptidoglycan-binding domain of MotB to become active stators as well as proton channels. MotB consists of 309 residues, forming a single transmembrane helix (30-50), a stalk (51-100) and a C-terminal peptidoglycan-binding domain (101-309). Although the stalk is dispensable for torque generation by the motor, it is required for efficient motor performance. Residues 51 to 72 prevent premature proton leakage through the proton channel prior to stator assembly into the motor. However, the role of residues 72-100 remains unknown. Here, we analyzed the torque-speed relationship of the MotB(Δ72-100) motor. At a low speed near stall, this mutant motor produced torque at the wild-type level. Unlike the wild-type motor, however, torque dropped off drastically by slight decrease in external load and then showed a slow exponential decay over a wide range of load by its further reduction. Since it is known that the stator is a mechano-sensor and that the number of active stators changes in a load-dependent manner, we interpreted this unusual torque-speed relationship as anomaly in load-dependent control of the number of active stators. The results suggest that residues 72-100 of MotB is required for proper load-dependent control of the number of active stators around the rotor.
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