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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

Author

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  • Ryohei Yasuda

    (CREST ‘Genetic Programming’ Team 13, Teikyo University Biotechnology Center 3F, Nogawa 907, Miyamae-Ku
    Faculty of Science and Technology, Keio University
    Cold Spring Harbor Laboratory)

  • Hiroyuki Noji

    (CREST ‘Genetic Programming’ Team 13, Teikyo University Biotechnology Center 3F, Nogawa 907, Miyamae-Ku)

  • Masasuke Yoshida

    (CREST ‘Genetic Programming’ Team 13, Teikyo University Biotechnology Center 3F, Nogawa 907, Miyamae-Ku
    Chemical Resources Laboratory, Tokyo Institute of Technology)

  • Kazuhiko Kinosita

    (CREST ‘Genetic Programming’ Team 13, Teikyo University Biotechnology Center 3F, Nogawa 907, Miyamae-Ku
    Faculty of Science and Technology, Keio University)

  • Hiroyasu Itoh

    (CREST ‘Genetic Programming’ Team 13, Teikyo University Biotechnology Center 3F, Nogawa 907, Miyamae-Ku
    Tsukuba Research Laboratory, Hamamatsu Photonics KK, Tokodai)

Abstract

The enzyme F1-ATPase has been shown to be a rotary motor in which the central γ-subunit rotates inside the cylinder made of α3β3 subunits. At low ATP concentrations, the motor rotates in discrete 120° steps, consistent with sequential ATP hydrolysis on the three β-subunits. The mechanism of stepping is unknown. Here we show by high-speed imaging that the 120° step consists of roughly 90° and 30° substeps, each taking only a fraction of a millisecond. ATP binding drives the 90° substep, and the 30° substep is probably driven by release of a hydrolysis product. The two substeps are separated by two reactions of about 1 ms, which together occupy most of the ATP hydrolysis cycle. This scheme probably applies to rotation at full speed (∼130 revolutions per second at saturating ATP) down to occasional stepping at nanomolar ATP concentrations, and supports the binding-change model for ATP synthesis by reverse rotation of F1-ATPase.

Suggested Citation

  • Ryohei Yasuda & Hiroyuki Noji & Masasuke Yoshida & Kazuhiko Kinosita & Hiroyasu Itoh, 2001. "Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase," Nature, Nature, vol. 410(6831), pages 898-904, April.
    • Handle: RePEc:nat:nature:v:410:y:2001:i:6831:d:10.1038_35073513
    DOI: 10.1038/35073513
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    Cited by:

    1. 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.
    2. Leonie Vollmar & Julia Schimpf & Bianca Hermann & Thorsten Hugel, 2024. "Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    3. 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.
    4. Yan Kuai & Junxue Chen & Zetao Fan & Gang Zou & Joseph. R. Lakowicz & Douguo Zhang, 2021. "Planar photonic chips with tailored angular transmission for high-contrast-imaging devices," Nature Communications, Nature, vol. 12(1), pages 1-9, December.

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