ArticleJournal of bacteriology2013
Distinct roles of highly conserved charged residues at the MotA-FliG interface in bacterial flagellar motor rotation.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
46 citing papers in PubMed, 83 citations in OpenAlex.
- Genetic analysis of flagellar-mediated surface sensing byJournal of bacteriology · 2025Article
- Viscosity-dependent determinants ofmBio · 2024Article
- Article
- 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
- Flagellar brake protein YcgR interacts with motor proteins MotA and FliG to regulate the flagellar rotation speed and direction.Frontiers in microbiology · 2023Article
- Interference of flagellar rotation up-regulates the expression of small RNA contributing toScience advances · 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
- Human Pleural Fluid and Human Serum Albumin Modulate the Behavior of a Hypervirulent and Multidrug-Resistant (MDR)Pathogens (Basel, Switzerland) · 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
- Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation.Nature microbiology · 2020Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- Living in a Foster Home: The Single Subpolar Flagellum Fla1 ofBiomolecules · 2020Review
- Functional Regulators of Bacterial Flagella.Annual review of microbiology · 2019Review
- Article
- Flagella-Driven Motility of Bacteria.Biomolecules · 2019Review
- Novel Insights into Conformational Rearrangements of the Bacterial Flagellar Switch Complex.mBio · 2019Article
- Effect of the MotA(M206I) Mutation on Torque Generation and Stator Assembly in theJournal of bacteriology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Electrostatic interactions between the stator protein MotA and the rotor protein FliG are important for bacterial flagellar motor rotation. Arg90 and Glu98 of MotA are required not only for torque generation but also for stator assembly around the rotor, but their actual roles remain unknown. Here we analyzed the roles of functionally important charged residues at the MotA-FliG interface in motor performance. About 75% of the motA(R90E) cells and 45% of the motA(E98K) cells showed no fluorescent spots of green fluorescent protein (GFP)-MotB, indicating reduced efficiency of stator assembly around the rotor. The FliG(D289K) and FliG(R281V) mutations, which restore the motility of the motA(R90E) and motA(E98K) mutants, respectively, showed reduced numbers and intensity of GFP-MotB spots as well. The FliG(D289K) mutation significantly recovered the localization of GFP-MotB to the motor in the motA(R90E) mutant, whereas the FliG(R281V) mutation did not recover the GFP-MotB localization in the motA(E98K) mutant. These results suggest that the MotA-Arg90-FliG-Asp289 interaction is critical for the proper positioning of the stators around the rotor, whereas the MotA-Glu98-FliG-Arg281 interaction is more important for torque generation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.