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Shaping the mitochondrial proteome.

Toni Gabaldón1, Martijn A Huynen

  • 1NCMLS, Nijmegen Center for Molecular Life Sciences, P/O: CMBI, Center for Molecular and Biomolecular Informatics, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands. T.Gabaldon@cmbi.ru.nl

Biochimica Et Biophysica Acta
|December 4, 2004
PubMed
Summary
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Mitochondria evolved from bacteria, with most of their proteins now being of eukaryotic origin, not from the original endosymbiont. This proteome evolution highlights their specialized functions in eukaryotic metabolism.

Area of Science:

  • Cell Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Mitochondria originated from a bacterial endosymbiont ~2 billion years ago.
  • The mitochondrial proteome has undergone extensive changes since endosymbiosis.
  • Only a small fraction of mitochondrial proteins are derived from the ancestral endosymbiont.

Purpose of the Study:

  • To review recent advances in understanding mitochondrial proteome origin and evolution.
  • To explore the extensive protein renewal and recruitment in mitochondria.
  • To shed light on the transformation of mitochondria into specialized eukaryotic organelles.

Main Methods:

  • Comparative genomics
  • Proteomics
  • Literature review of recent advances

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Main Results:

  • Mitochondrial proteome renewal is extensive, with only 14-16% traceable to the bacterial endosymbiont.
  • New eukaryotic complexes, like ATP/ADP translocase and import machinery, have been incorporated.
  • The majority of mitochondrial proteins are of diverse, recruited eukaryotic origin.

Conclusions:

  • Mitochondrial proteome composition reflects a deep evolutionary transformation.
  • Mitochondria have evolved specialized functions beyond ATP production within eukaryotic metabolism.
  • Comparative genomics and proteomics are key to unraveling mitochondrial evolution.