ArticleNature communications2021
Cooperative stator assembly of bacterial flagellar motor mediated by rotation.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Dynamic velocity response of E. coli powered by proteorhodopsin.Biophysical reports · 2026Article
- Signature of cooperativity in the stochastic fluctuations of small systems with application to the bacterial flagellar motor.Scientific reports · 2025Article
- Scrutinizing Stator Rotation in the Bacterial Flagellum: Reconciling Experiments and Switching Models.Biomolecules · 2025Review
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- Ion selectivity and rotor coupling of the Vibrio flagellar sodium-driven stator unit.Nature communications · 2023Article
- A multi-state dynamic process confers mechano-adaptation to a biological nanomachine.Nature communications · 2022Article
- Relaxation time asymmetry in stator dynamics of the bacterial flagellar motor.Science advances · 2022Article
- FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A new class of biological ion-driven rotary molecular motors with 5:2 symmetry.Frontiers in microbiology · 2022Review
- Cooperative stator assembly of bacterial flagellar motor mediated by rotation.Nature communications · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cooperativity has a central place in biological regulation, providing robust and highly-sensitive regulation. The bacterial flagellar motor implements autonomous torque regulation based on the stator's dynamic structure; the stator units bind to and dissociate from the motor dynamically in response to environmental changes. However, the mechanism of this dynamic assembly is not fully understood. Here, we demonstrate the cooperativity in the stator assembly dynamics. The binding is slow at the stalled state, but externally forced rotation as well as driving by motor torque in either direction boosts the stator binding. Hence, once a stator unit binds, it drives the rotor and triggers the avalanche of succeeding bindings. This cooperative mechanism based on nonequilibrium allostery accords with the recently-proposed gear-type coupling between the rotor and stator.
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