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Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio

Author

Listed:
  • William S. Ryu

    (Harvard University
    Rowland Institute for Science)

  • Richard M. Berry

    (The Randall Centre, King's College London)

  • Howard C. Berg

    (Harvard University
    Rowland Institute for Science)

Abstract

Rotation of the bacterial flagellar motor is driven by an ensemble of torque-generating units containing the proteins MotA and MotB1,2,3. Here, by inducing expression of MotA in motA- cells under conditions of low viscous load, we show that the limiting speed of the motor is independent of the number of units: at vanishing load, one unit turns the motor as rapidly as many. This result indicates that each unit may remain attached to the rotor for most of its mechanochemical cycle, that is, that it has a high duty ratio4. Thus, torque generators behave more like kinesin, the protein that moves vesicles along microtubules, than myosin, the protein that powers muscle. However, their translation rates, stepping frequencies and power outputs are much higher, being greater than 30 µm s-1, 12 kHz and 1.5 × 105 pN nm s-1, respectively.

Suggested Citation

  • William S. Ryu & Richard M. Berry & Howard C. Berg, 2000. "Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio," Nature, Nature, vol. 403(6768), pages 444-447, January.
    • Handle: RePEc:nat:nature:v:403:y:2000:i:6768:d:10.1038_35000233
    DOI: 10.1038/35000233
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    Cited by:

    1. Navish Wadhwa & Alberto Sassi & Howard C. Berg & Yuhai Tu, 2022. "A multi-state dynamic process confers mechano-adaptation to a biological nanomachine," Nature Communications, Nature, vol. 13(1), pages 1-9, December.

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