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Direct observation of the rotation of F1-ATPase

Author

Listed:
  • Hiroyuki Noji

    (Tokyo Institute of Technology)

  • Ryohei Yasuda

    (Keio University)

  • Masasuke Yoshida

    (Tokyo Institute of Technology)

  • Kazuhiko Kinosita

    (Keio University)

Abstract

Cells employ a variety of linear motors, such as myosin1–3, kinesin4 and RNA polymerase5, which move along and exert force on a filamentous structure. But only one rotary motor has been investigated in detail, the bacterial flagellum6 (a complex of about 100 protein molecules7). We now show that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion. A central rotor of radius ∼1 nm, formed by its γ-subunit, turns in a stator barrel of radius ∼5nm formed by three α- and three β-subunits8. F1 ATPase, together with the membrane-embedded proton-conducting unit F0, forms the H+-ATP synthase that reversibly couples transmembrane proton flow to ATP synthesis/hydrolysis in respiring and photosynthetic cells9,10. It has been suggested that the γ-subunit of F1-ATPase rotates within the αβ-hexamer11, a conjecture supported by structural8, biochemical12,13 and spectroscopic14 studies. We attached a fluorescent actin filament to the γ-subunit as a marker, which enabled us to observe this motion directly. In the presence of ATP, the filament rotated for more than 100 revolutions in an anticlockwise direction when viewed from the 'membrane' side. The rotary torque produced reached more than 40 pN nm −l under high load.

Suggested Citation

  • Hiroyuki Noji & Ryohei Yasuda & Masasuke Yoshida & Kazuhiko Kinosita, 1997. "Direct observation of the rotation of F1-ATPase," Nature, Nature, vol. 386(6622), pages 299-302, March.
  • Handle: RePEc:nat:nature:v:386:y:1997:i:6622:d:10.1038_386299a0
    DOI: 10.1038/386299a0
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    Citations

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    Cited by:

    1. Alex Albaugh & Todd R. Gingrich, 2022. "Simulating a chemically fueled molecular motor with nonequilibrium molecular dynamics," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. Eva Bertosin & Christopher M. Maffeo & Thomas Drexler & Maximilian N. Honemann & Aleksei Aksimentiev & Hendrik Dietz, 2021. "A nanoscale reciprocating rotary mechanism with coordinated mobility control," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    3. Ryohei Kobayashi & Hiroshi Ueno & Kei-ichi Okazaki & Hiroyuki Noji, 2023. "Molecular mechanism on forcible ejection of ATPase inhibitory factor 1 from mitochondrial ATP synthase," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. J. Kishikawa & A. Nakanishi & A. Nakano & S. Saeki & A. Furuta & T. Kato & K. Mistuoka & K. Yokoyama, 2022. "Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    5. Ryojun Toyoda & Nong V. Hoang & Kiana Gholamjani Moghaddam & Stefano Crespi & Daisy R. S. Pooler & Shirin Faraji & Maxim S. Pshenichnikov & Ben L. Feringa, 2022. "Synergistic interplay between photoisomerization and photoluminescence in a light-driven rotary molecular motor," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    6. Atsuki Nakano & Jun-ichi Kishikawa & Kaoru Mitsuoka & Ken Yokoyama, 2023. "Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    7. Zhang, Yunxin, 2009. "A general two-cycle network model of molecular motors," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 388(17), pages 3465-3474.

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