ArticleNature communications2022
A multi-state dynamic process confers mechano-adaptation to a biological nanomachine.
Article in Nature communications, 2022. 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.
- Long-range coupling regulates stator dynamics in the bacterial flagellar motor.bioRxiv : the preprint server for biology · 2025Article
- 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
- Physical mechanism reveals bacterial slowdown above a critical number of flagella.Journal of the Royal Society, Interface · 2024Article
- Structural basis of directional switching by the bacterial flagellum.Nature microbiology · 2024Article
- Motility inMicroorganisms · 2023Article
- Flagellar motors of swimming bacteria contain an incomplete set of stator units to ensure robust motility.Science advances · 2023Article
- Structural Basis of Directional Switching by the Bacterial Flagellum.Research square · 2023Article
- Ion selectivity and rotor coupling of the Vibrio flagellar sodium-driven stator unit.Nature communications · 2023Article
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4 authors.
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Abstract
Adaptation is a defining feature of living systems. The bacterial flagellar motor adapts to changes in the external mechanical load by adding or removing torque-generating (stator) units. But the molecular mechanism behind this mechano-adaptation remains unclear. Here, we combine single motor eletrorotation experiments and theoretical modeling to show that mechano-adaptation of the flagellar motor is enabled by multiple mechanosensitive internal states. Dwell time statistics from experiments suggest the existence of at least two bound states with a high and a low unbinding rate, respectively. A first-passage-time analysis of a four-state model quantitatively explains the experimental data and determines the transition rates among all four states. The torque generated by bound stator units controls their effective unbinding rate by modulating the transition between the bound states, possibly via a catch bond mechanism. Similar force-mediated feedback enabled by multiple internal states may apply to adaptation in other macromolecular complexes.
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