IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v614y2023i7946d10.1038_s41586-022-05641-w.html
   My bibliography  Save this article

Mitochondrial complexome reveals quality-control pathways of protein import

Author

Listed:
  • Uwe Schulte

    (University of Freiburg
    University of Freiburg)

  • Fabian den Brave

    (University of Bonn)

  • Alexander Haupt

    (University of Freiburg)

  • Arushi Gupta

    (University of Bonn
    University of Freiburg)

  • Jiyao Song

    (University of Bonn
    University of Freiburg)

  • Catrin S. Müller

    (University of Freiburg)

  • Jeannine Engelke

    (University of Bonn)

  • Swadha Mishra

    (University of Bonn)

  • Christoph Mårtensson

    (University of Freiburg
    MTIP)

  • Lars Ellenrieder

    (University of Freiburg
    Novartis)

  • Chantal Priesnitz

    (University of Freiburg)

  • Sebastian P. Straub

    (University of Freiburg
    University of Freiburg
    Sanofi-Aventis (Suisse))

  • Kim Nguyen Doan

    (University of Freiburg)

  • Bogusz Kulawiak

    (University of Freiburg
    Polish Academy of Sciences)

  • Wolfgang Bildl

    (University of Freiburg)

  • Heike Rampelt

    (University of Freiburg
    University of Freiburg)

  • Nils Wiedemann

    (University of Freiburg
    University of Freiburg
    University of Freiburg)

  • Nikolaus Pfanner

    (University of Freiburg
    University of Freiburg
    University of Freiburg)

  • Bernd Fakler

    (University of Freiburg
    University of Freiburg
    Center for Basics in NeuroModulation)

  • Thomas Becker

    (University of Bonn)

Abstract

Mitochondria have crucial roles in cellular energetics, metabolism, signalling and quality control1–4. They contain around 1,000 different proteins that often assemble into complexes and supercomplexes such as respiratory complexes and preprotein translocases1,3–7. The composition of the mitochondrial proteome has been characterized1,3,5,6; however, the organization of mitochondrial proteins into stable and dynamic assemblies is poorly understood for major parts of the proteome1,4,7. Here we report quantitative mapping of mitochondrial protein assemblies using high-resolution complexome profiling of more than 90% of the yeast mitochondrial proteome, termed MitCOM. An analysis of the MitCOM dataset resolves >5,200 protein peaks with an average of six peaks per protein and demonstrates a notable complexity of mitochondrial protein assemblies with distinct appearance for respiration, metabolism, biogenesis, dynamics, regulation and redox processes. We detect interactors of the mitochondrial receptor for cytosolic ribosomes, of prohibitin scaffolds and of respiratory complexes. The identification of quality-control factors operating at the mitochondrial protein entry gate reveals pathways for preprotein ubiquitylation, deubiquitylation and degradation. Interactions between the peptidyl-tRNA hydrolase Pth2 and the entry gate led to the elucidation of a constitutive pathway for the removal of preproteins. The MitCOM dataset—which is accessible through an interactive profile viewer—is a comprehensive resource for the identification, organization and interaction of mitochondrial machineries and pathways.

Suggested Citation

  • Uwe Schulte & Fabian den Brave & Alexander Haupt & Arushi Gupta & Jiyao Song & Catrin S. Müller & Jeannine Engelke & Swadha Mishra & Christoph Mårtensson & Lars Ellenrieder & Chantal Priesnitz & Sebas, 2023. "Mitochondrial complexome reveals quality-control pathways of protein import," Nature, Nature, vol. 614(7946), pages 153-159, February.
  • Handle: RePEc:nat:nature:v:614:y:2023:i:7946:d:10.1038_s41586-022-05641-w
    DOI: 10.1038/s41586-022-05641-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41586-022-05641-w
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/s41586-022-05641-w?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Qilin Zhang & Ziyan Xu & Rui Han & Yunzhi Wang & Zhen Ye & Jiajun Zhu & Yixin Cai & Fan Zhang & Jiangyan Zhao & Boyuan Yao & Zhaoyu Qin & Nidan Qiao & Ruofan Huang & Jinwen Feng & Yongfei Wang & Wenti, 2024. "Proteogenomic characterization of skull-base chordoma," Nature Communications, Nature, vol. 15(1), pages 1-32, December.
    2. Wen Fang & Liu Jiang & Yibing Zhu & Sen Yang & Hong Qiu & Jiou Cheng & Qingxi Liang & Zong-cai Tu & Cunqi Ye, 2023. "Methionine restriction constrains lipoylation and activates mitochondria for nitrogenic synthesis of amino acids," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:614:y:2023:i:7946:d:10.1038_s41586-022-05641-w. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.