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Stoichiometry and turnover in single, functioning membrane protein complexes.

Mark C Leake1, Jennifer H Chandler, George H Wadhams

  • 1Clarendon Laboratory, Department of Physics, University of Oxford, Parks Road, Oxford OX1 3PU, UK.

Nature
|September 15, 2006
PubMed
Summary
This summary is machine-generated.

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The bacterial flagellar motor uses about 22 MotB protein subunits per motor, with rapid turnover from a membrane pool. This study precisely measures the number and dynamics of these essential motor components.

Area of Science:

  • Cellular biology
  • Molecular machines
  • Bacterial motility

Background:

  • Cell membrane proteins drive essential cellular functions.
  • The bacterial flagellar motor is an ion-driven rotary machine enabling cell propulsion.
  • MotB is a key stator component, coupling ion flow to torque and anchoring to the cell wall.

Purpose of the Study:

  • To investigate the protein stoichiometry, dynamics, and turnover of MotB in functioning bacterial flagellar motors.
  • To precisely quantify MotB molecules within the motor and in the surrounding membrane.
  • To determine the rate of MotB subunit exchange within the flagellar motor.

Main Methods:

  • Utilized single-molecule precision techniques in live Escherichia coli.
  • Monitored flagellar motor function via tethered cell rotation.

Related Experiment Videos

  • Employed total internal reflection fluorescence microscopy to track green fluorescent protein-labeled MotB (GFP-MotB).
  • Quantified GFP-MotB using stepwise photobleaching and assessed dynamics via fluorescence recovery after photobleaching and fluorescence loss in photobleaching.

    • Main Results:

    • Each flagellar motor contains approximately 22 copies of GFP-MotB, suggesting 11 stators with two MotB molecules each.
    • A membrane pool of roughly 200 GFP-MotB molecules was observed, diffusing at ~0.008 µm²/s.
    • MotB demonstrated rapid turnover between the membrane pool and motor, with a rate constant of ~0.04 s⁻¹, indicating a dwell time of approximately 0.5 minutes.

    Conclusions:

    • This study provides the first direct measurement of protein subunit stoichiometry and rapid turnover in a functioning molecular machine.
    • The findings reveal dynamic assembly and disassembly of MotB within the bacterial flagellar motor stator.
    • Understanding MotB dynamics is crucial for comprehending flagellar motor function and regulation.