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The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase

Author

Listed:
  • Jiyao Song

    (University of Bonn
    University of Freiburg)

  • Liesa Steidle

    (University of Freiburg)

  • Isabelle Steymans

    (University of Bonn)

  • Jasjot Singh

    (University of Bonn)

  • Anne Sanner

    (University of Bonn)

  • Lena Böttinger

    (University of Freiburg)

  • Dominic Winter

    (University of Bonn)

  • Thomas Becker

    (University of Bonn)

Abstract

The mitochondrial F1FO-ATP synthase produces the bulk of cellular ATP. The soluble F1 domain contains the catalytic head that is linked via the central stalk and the peripheral stalk to the membrane embedded rotor of the FO domain. The assembly of the F1 domain and its linkage to the peripheral stalk is poorly understood. Here we show a dual function of the mitochondrial Hsp70 (mtHsp70) in the formation of the ATP synthase. First, it cooperates with the assembly factors Atp11 and Atp12 to form the F1 domain of the ATP synthase. Second, the chaperone transfers Atp5 into the assembly line to link the catalytic head with the peripheral stalk. Inactivation of mtHsp70 leads to integration of assembly-defective Atp5 variants into the mature complex, reflecting a quality control function of the chaperone. Thus, mtHsp70 acts as an assembly and quality control factor in the biogenesis of the F1FO-ATP synthase.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-022-35720-5
    DOI: 10.1038/s41467-022-35720-5
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    References listed on IDEAS

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    1. Alexander Benjamin Schendzielorz & Piotr Bragoszewski & Nataliia Naumenko & Ridhima Gomkale & Christian Schulz & Bernard Guiard & Agnieszka Chacinska & Peter Rehling, 2018. "Motor recruitment to the TIM23 channel’s lateral gate restricts polypeptide release into the inner membrane," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    2. 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.
    3. Wolfgang Junge & Hendrik Sielaff & Siegfried Engelbrecht, 2009. "Torque generation and elastic power transmission in the rotary FOF1-ATPase," Nature, Nature, vol. 459(7245), pages 364-370, May.
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