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<p>Mitochondria are essential organelles whose functions depend on coordinated multiprotein complexes, yet their composition and organization remain incomplete. Here, we present a large-scale map of mitochondrial protein complexes by integrating affinity purification of 740 endogenously GFP-tagged mitochondrial proteins with biochemical co-fractionation of mitochondrial extracts from yeast (<i>Saccharomyces cerevisiae</i>) grown under respiratory conditions. Mass spectrometry identifies 13,716 high-confidence protein associations and defines 556 heteromeric complexes, many previously unknown. These assemblies reveal factors involved in coenzyme Q6 biosynthesis, membrane contact sites, phospholipid transport, and coordination with the MICOS complex during respiration. We further link 538 assemblies to 294 candidate human disease genes and construct a conservation map of 852,146 predicted mitochondrial interactions across 271 genomes, and validate key predictions in human cell lines and mouse brain tissue. Together, this work provides a comprehensive mitochondrial interactome, assigning functions to poorly characterized proteins, and offering insights into mitochondrial biology and disease-associated assemblies.</p>

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Global mitochondrial connectivity map reveals the landscape of yeast functional assemblies and conserved protein communities

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年5月5日

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  • Matthew Jessulat,
  • Sadhna Phanse,
  • Hiroyuki Aoki,
  • Kirsten Broderick,
  • Qingzhou Zhang,
  • Inês Gomes Castro,
  • Noelle Alexa Novales,
  • Sakib Abrar Hossain,
  • Tatiana Saccon,
  • Mohamed Taha Moutaoufik,
  • Thomson Patrick Joseph,
  • Shahreen Amin,
  • Larrisa Hoell,
  • Zoran Minic,
  • Yury Bykov,
  • Noga Preminger,
  • Sahily Gonzalez Crespo,
  • Jamie Snider,
  • Ashkan Golshani,
  • Igor Stagljar,
  • Jose R. Rodriguez-Medina,
  • Catherine F. Clarke,
  • Maya Schuldiner,
  • Mohan Babu

摘要

Mitochondria are essential organelles whose functions depend on coordinated multiprotein complexes, yet their composition and organization remain incomplete. Here, we present a large-scale map of mitochondrial protein complexes by integrating affinity purification of 740 endogenously GFP-tagged mitochondrial proteins with biochemical co-fractionation of mitochondrial extracts from yeast (Saccharomyces cerevisiae) grown under respiratory conditions. Mass spectrometry identifies 13,716 high-confidence protein associations and defines 556 heteromeric complexes, many previously unknown. These assemblies reveal factors involved in coenzyme Q6 biosynthesis, membrane contact sites, phospholipid transport, and coordination with the MICOS complex during respiration. We further link 538 assemblies to 294 candidate human disease genes and construct a conservation map of 852,146 predicted mitochondrial interactions across 271 genomes, and validate key predictions in human cell lines and mouse brain tissue. Together, this work provides a comprehensive mitochondrial interactome, assigning functions to poorly characterized proteins, and offering insights into mitochondrial biology and disease-associated assemblies.