ArticleProceedings of the National Academy of Sciences of the United States of America2016
Internal and external components of the bacterial flagellar motor rotate as a unit.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Torque-generating units of the bacterial flagellar motor are rotary motors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Scrutinizing Stator Rotation in the Bacterial Flagellum: Reconciling Experiments and Switching Models.Biomolecules · 2025Review
- Synchronized strobed phase contrast and fluorescence microscopy: the interlaced standard reimagined.Optics express · 2023Article
- Bacterial motility: machinery and mechanisms.Nature reviews. Microbiology · 2022Review
- How the PhoP/PhoQ System Controls Virulence and MgMicrobiology and molecular biology reviews : MMBR · 2021Review
- Motile ghosts of the halophilic archaeon,Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- New Twists and Turns in Bacterial Locomotion and Signal Transduction.Journal of bacteriology · 2019Review
- CW and CCW Conformations of the E. coli Flagellar Motor C-Ring Evaluated by Fluorescence Anisotropy.Biophysical journal · 2018Article
- MotI (DgrA) acts as a molecular clutch on the flagellar stator protein MotA inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Impact of fluorescent protein fusions on the bacterial flagellar motor.Scientific reports · 2017Article
- The flagellar motor adapts, optimizing bacterial behavior.Protein science : a publication of the Protein Society · 2017Review
- Length-dependent flagellar growth ofeLife · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Most bacteria that swim, including Escherichia coli, are propelled by helical filaments, each driven at its base by a rotary motor powered by a proton or a sodium ion electrochemical gradient. Each motor contains a number of stator complexes, comprising 4MotA 2MotB or 4PomA 2PomB, proteins anchored to the rigid peptidoglycan layer of the cell wall. These proteins exert torque on a rotor that spans the inner membrane. A shaft connected to the rotor passes through the peptidoglycan and the outer membrane through bushings, the P and L rings, connecting to the filament by a flexible coupling known as the hook. Although the external components, the hook and the filament, are known to rotate, having been tethered to glass or marked by latex beads, the rotation of the internal components has remained only a reasonable assumption. Here, by using polarized light to bleach and probe an internal YFP-FliN fusion, we show that the innermost components of the cytoplasmic ring rotate at a rate similar to that of the hook.
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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.