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

Ryohei Kobayashi, Hiroshi Ueno, Kei-ichi Okazaki and Hiroyuki Noji ()
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Ryohei Kobayashi: Graduate School of Engineering, The University of Tokyo
Hiroshi Ueno: Graduate School of Engineering, The University of Tokyo
Kei-ichi Okazaki: Institute for Molecular Science
Hiroyuki Noji: Graduate School of Engineering, The University of Tokyo

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-37182-9

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