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Torque, but not FliL, regulates mechanosensitive flagellar motor-function.

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Area of Science:

  • Microbiology
  • Biophysics
  • Molecular Biology

Background:

  • The bacterial flagellar motor's stator complex is crucial for motility and surface sensing.
  • Stator units adapt to increased viscous loads by remodeling and recruiting more units.

Purpose of the Study:

  • To investigate if the torque generated by individual stator units influences their binding to the rotor.
  • To determine the role of FliL in stator-rotor association and motor torque generation.

Main Methods:

  • Measuring stator-rotor binding in various mutant strains, including a fliL deletion mutant and a paralyzed mutant.
  • Developing and applying an analytical model to describe stator-rotor binding dynamics based on force generation.

Main Results:

  • Contrary to previous reports, the fliL mutant showed wildtype torque and stator-binding at high loads.
  • Stator-rotor binding was significantly weaker in paralyzed motors unable to generate torque.
  • The analytical model accurately predicted stator-rotor binding based on force-dependent dissociation rates.

Conclusions:

  • Stator unit binding to the rotor is enhanced by the force each unit generates.
  • The force-dependent binding mechanism is a key factor in regulating bacterial flagellar motor function.
  • FliL does not play a significant role in the motor function of E. coli.