|Title||Shaping the mitochondrial proteome|
|Publication Type||Journal Article|
|Year of Publication||2004|
|Authors||Gabaldón, T, Huynen, MA|
|Journal||Biochim Biophys Acta|
|Keywords||Animals Biological Transport Energy Metabolism Eukaryotic Cells/physiology *Evolution Humans Mitochondria/*physiology Phylogeny Proteome/*physiology|
Mitochondria are eukaryotic organelles that originated from a single bacterial endosymbiosis some 2 billion years ago. The transition from the ancestral endosymbiont to the modern mitochondrion has been accompanied by major changes in its protein content, the so-called proteome. These changes included complete loss of some bacterial pathways, amelioration of others and gain of completely new complexes of eukaryotic origin such as the ATP/ADP translocase and most of the mitochondrial protein import machinery. This renewal of proteins has been so extensive that only 14-16% of modern mitochondrial proteome has an origin that can be traced back to the bacterial endosymbiont. The rest consists of proteins of diverse origin that were eventually recruited to function in the organelle. This shaping of the proteome content reflects the transformation of mitochondria into a highly specialized organelle that, besides ATP production, comprises a variety of functions within the eukaryotic metabolism. Here we review recent advances in the fields of comparative genomics and proteomics that are throwing light on the origin and evolution of the mitochondrial proteome.
Gabaldon, Toni Huynen, Martijn A Research Support, Non-U.S. Gov’t Review Netherlands Biochimica et biophysica acta Biochim Biophys Acta. 2004 Dec 6;1659(2-3):212-20.