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Molecular mechanism on forcible ejection of ATPase inhibitory factor 1 from mitochondrial ATP synthase

Author

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  • Ryohei Kobayashi

    (Graduate School of Engineering, The University of Tokyo
    Institute for Molecular Science)

  • Hiroshi Ueno

    (Graduate School of Engineering, The University of Tokyo)

  • Kei-ichi Okazaki

    (Institute for Molecular Science
    The Graduate University for Advanced Studies, SOKENDAI)

  • Hiroyuki Noji

    (Graduate School of Engineering, The University of Tokyo)

Abstract

IF1 is a natural inhibitor protein for mitochondrial FoF1 ATP synthase that blocks catalysis and rotation of the F1 by deeply inserting its N-terminal helices into F1. A unique feature of IF1 is condition-dependent inhibition; although IF1 inhibits ATP hydrolysis by F1, IF1 inhibition is relieved under ATP synthesis conditions. To elucidate this condition-dependent inhibition mechanism, we have performed single-molecule manipulation experiments on IF1-inhibited bovine mitochondrial F1 (bMF1). The results show that IF1-inhibited F1 is efficiently activated only when F1 is rotated in the clockwise (ATP synthesis) direction, but not in the counterclockwise direction. The observed rotational-direction-dependent activation explains the condition-dependent mechanism of IF1 inhibition. Investigation of mutant IF1 with N-terminal truncations shows that the interaction with the γ subunit at the N-terminal regions is crucial for rotational-direction-dependent ejection, and the middle long helix is responsible for the inhibition of F1.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-37182-9
    DOI: 10.1038/s41467-023-37182-9
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    References listed on IDEAS

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    1. Meghna Sobti & Hiroshi Ueno & Hiroyuki Noji & Alastair G. Stewart, 2021. "The six steps of the complete F1-ATPase rotary catalytic cycle," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. 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.
    3. Rikiya Watanabe & Hiroyuki Noji, 2014. "Timing of inorganic phosphate release modulates the catalytic activity of ATP-driven rotary motor protein," Nature Communications, Nature, vol. 5(1), pages 1-7, May.
    4. Hui Guo & Gautier M. Courbon & Stephanie A. Bueler & Juntao Mai & Jun Liu & John L. Rubinstein, 2021. "Structure of mycobacterial ATP synthase bound to the tuberculosis drug bedaquiline," Nature, Nature, vol. 589(7840), pages 143-147, January.
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