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Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex

Author

Listed:
  • Corey F. Hryc

    (McGovern Medical School at the University of Texas Health Science Center)

  • Venkata K. P. S. Mallampalli

    (McGovern Medical School at the University of Texas Health Science Center)

  • Evgeniy I. Bovshik

    (McGovern Medical School at the University of Texas Health Science Center)

  • Stavros Azinas

    (McGovern Medical School at the University of Texas Health Science Center)

  • Guizhen Fan

    (McGovern Medical School at the University of Texas Health Science Center)

  • Irina I. Serysheva

    (McGovern Medical School at the University of Texas Health Science Center)

  • Genevieve C. Sparagna

    (University of Colorado Anschutz Medical Campus)

  • Matthew L. Baker

    (McGovern Medical School at the University of Texas Health Science Center)

  • Eugenia Mileykovskaya

    (McGovern Medical School at the University of Texas Health Science Center)

  • William Dowhan

    (McGovern Medical School at the University of Texas Health Science Center)

Abstract

Cardiolipin is a hallmark phospholipid of mitochondrial membranes. Despite established significance of cardiolipin in supporting respiratory supercomplex organization, a mechanistic understanding of this lipid-protein interaction is still lacking. To address the essential role of cardiolipin in supercomplex organization, we report cryo-EM structures of a wild type supercomplex (IV1III2IV1) and a supercomplex (III2IV1) isolated from a cardiolipin-lacking Saccharomyces cerevisiae mutant at 3.2-Å and 3.3-Å resolution, respectively, and demonstrate that phosphatidylglycerol in III2IV1 occupies similar positions as cardiolipin in IV1III2IV1. Lipid-protein interactions within these complexes differ, which conceivably underlies the reduced level of IV1III2IV1 and high levels of III2IV1 and free III2 and IV in mutant mitochondria. Here we show that anionic phospholipids interact with positive amino acids and appear to nucleate a phospholipid domain at the interface between the individual complexes, which dampen charge repulsion and further stabilize interaction, respectively, between individual complexes.

Suggested Citation

  • Corey F. Hryc & Venkata K. P. S. Mallampalli & Evgeniy I. Bovshik & Stavros Azinas & Guizhen Fan & Irina I. Serysheva & Genevieve C. Sparagna & Matthew L. Baker & Eugenia Mileykovskaya & William Dowha, 2023. "Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38441-5
    DOI: 10.1038/s41467-023-38441-5
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    References listed on IDEAS

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    1. Irene Vercellino & Leonid A. Sazanov, 2021. "Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV," Nature, Nature, vol. 598(7880), pages 364-367, October.
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    Cited by:

    1. Ana Paula Lobez & Fei Wu & Justin M. Di Trani & John L. Rubinstein & Mikael Oliveberg & Peter Brzezinski & Agnes Moe, 2024. "Electron transfer in the respiratory chain at low salinity," Nature Communications, Nature, vol. 15(1), pages 1-9, December.

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