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Related Experiment Videos

Rotation of Escherichia coli F(1)-ATPase.

H Noji1, K Häsler, W Junge

  • 1CREST team13 (Core Research for Evolutional Science and Technology) "Genetic Programming" Team 13, Teikyo University Biotechnology Research Center 3F, Nogawa 907, Kawasaki, Miyamae-ku, 216-0001, Japan.

Biochemical and Biophysical Research Communications
|July 15, 1999
PubMed
Summary

Researchers observed ATP-driven rotation in Escherichia coli F(1)-ATPase, mirroring findings in thermophilic F(1)-ATPase. This suggests that F(1)-ATPases share fundamental rotational properties across different biological sources.

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F1-ATPase: a highly coupled reversible rotary motor.

Biochemical Society transactions·2006

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • F(1)-ATPase is a molecular motor that synthesizes ATP.
  • Previous studies on thermophilic F(1)-ATPase (TF(1)) revealed its rotational mechanism.

Purpose of the Study:

  • To investigate the rotational properties of F(1)-ATPase from Escherichia coli.
  • To compare the rotational mechanism of E. coli F(1)-ATPase with that of TF(1).

Main Methods:

  • Utilized a method previously applied to TF(1) for observing rotation.
  • Attached a fluorescent actin filament to the gamma subunit of E. coli F(1)-ATPase.
  • Observed ATP-driven rotation using microscopy.

Main Results:

  • Demonstrated ATP-driven rotation of the actin filament in E. coli F(1)-ATPase.

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  • Measured torque and direction of rotation.
  • Observed identical torque values and rotational direction compared to TF(1).

    • Conclusions:

    • E. coli F(1)-ATPase exhibits rotational properties similar to TF(1).
    • F(1)-ATPases likely share conserved rotational mechanisms regardless of their source organism.