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INA complex liaises the F1Fo-ATP synthase membrane motor modules

Author

Listed:
  • Nataliia Naumenko

    (University Medical Center Göttingen, GZMB)

  • Marcel Morgenstern

    (University Freiburg)

  • Robert Rucktäschel

    (University Medical Center Göttingen, GZMB)

  • Bettina Warscheid

    (University Freiburg
    University of Freiburg)

  • Peter Rehling

    (University Medical Center Göttingen, GZMB
    Max Planck Institute for Biophysical Chemistry)

Abstract

The F1F0-ATP synthase translates a proton flux across the inner mitochondrial membrane into a mechanical rotation, driving anhydride bond formation in the catalytic portion. The complex’s membrane-embedded motor forms a proteinaceous channel at the interface between Atp9 ring and Atp6. To prevent unrestricted proton flow dissipating the H+-gradient, channel formation is a critical and tightly controlled step during ATP synthase assembly. Here we show that the INA complex (INAC) acts at this decisive step promoting Atp9-ring association with Atp6. INAC binds to newly synthesized mitochondrial-encoded Atp6 and Atp8 in complex with maturation factors. INAC association is retained until the F1-portion is built on Atp6/8 and loss of INAC causes accumulation of the free F1. An independent complex is formed between INAC and the Atp9 ring. We conclude that INAC maintains assembly intermediates of the F1 F0-ATP synthase in a primed state for the terminal assembly step–motor module formation.

Suggested Citation

  • Nataliia Naumenko & Marcel Morgenstern & Robert Rucktäschel & Bettina Warscheid & Peter Rehling, 2017. "INA complex liaises the F1Fo-ATP synthase membrane motor modules," Nature Communications, Nature, vol. 8(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01437-z
    DOI: 10.1038/s41467-017-01437-z
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    Cited by:

    1. Jiyao Song & Liesa Steidle & Isabelle Steymans & Jasjot Singh & Anne Sanner & Lena Böttinger & Dominic Winter & Thomas Becker, 2023. "The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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