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
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Cited by:
- 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.
- 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.
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