ArticleBiophysical journal2016
Bacterial Flagellar Motor Switch in Response to CheY-P Regulation and Motor Structural Alterations.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A magnetotactic bacterium capable of magnetic sensing.iScience · 2025Article
- Signature of cooperativity in the stochastic fluctuations of small systems with application to the bacterial flagellar motor.Scientific reports · 2025Article
- Structural insights into the mechanism of archaellar rotational switching.Nature communications · 2022Article
- Grounding cognition: heterarchical control mechanisms in biology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- Microfluidic techniques for separation of bacterial cells via taxis.Microbial cell (Graz, Austria) · 2020Review
- Effects of Advective-Diffusive Transport of Multiple Chemoattractants on Motility of Engineered Chemosensory Particles in Fluidic Environments.Entropy (Basel, Switzerland) · 2019Article
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Authors and funding
4 authors.
Funding
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Abstract
The bacterial flagellar motor (BFM) is a molecular machine that rotates the helical filaments and propels the bacteria swimming toward favorable conditions. In our previous works, we built a stochastic conformational spread model to explain the dynamic and cooperative behavior of BFM switching. Here, we extended this model to test whether it can explain the latest experimental observations regarding CheY-P regulation and motor structural adaptivity. We show that our model predicts a strong correlation between rotational direction and the number of CheY-Ps bound to the switch complex, in agreement with the latest finding from Fukuoka et al. It also predicts that the switching sensitivity of the BFM can be fine-tuned by incorporating additional units into the switch complex, as recently demonstrated by Yuan et al., who showed that stoichiometry of FliM undergoes dynamic change to maintain ultrasensitivity in the motor switching response. In addition, by locking some rotor switching units on the switch complex into the stable clockwise-only conformation, our model has accurately simulated recent experiments expressing clockwise-locked FliG(ΔPAA) into the switch complex and reproduced the increased switching rate of the motor.
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