Proteomes mitochondrial

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Gabaldon T, Huynen MA (2004) Shaping the mitochondrial proteome. Biochim Biophys Acta 1659 212-220... [Pg.65]

Posewitz MC, King PW, Smolinski SL, Zhang L, Seibert M, Ghirardi ML (2004) Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe]-hydrogenase. J Biol Chem 279 25711-25720 Prokisch H et al. (2004) Integrative analysis of the mitochondrial proteome in yeast. PLoS Biol 2 el60... [Pg.178]

The compartmentalization of energy generation provides a mechanism for the increased efficiency of high energy bond transfer to form the ultimate cellular fuel ATP, and has been the driving force behind the evolution of the mitochondrion. This viewpoint is supported by studies of the mitochondrial proteome, which have demonstrated that proteins of eubacterial origin predominantly... [Pg.255]

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Kurland CG, Andersson SG (2000) Origin and evolution of the mitochondrial proteome. Microbiol Mol Biol Rev 64 786-820... [Pg.54]

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Fig. 7.2. The vast majority of mitochondrial proteins did not originate from the ancestral a-proteobacterial endosymbiont but from a variety of eukaryotic, eubacterial, and archaeal sources (Gabaldon and Huynen 2004 Esser et al. 2004 Timmis et al. 2004). The evolution of mitochondria was not only accompanied by a substantial loss of superfluous genes, but also by the transfer of many a-proteobacterial genes into the nucleus. As a consequence, many a-proteobacterial proteins were retargeted to other cellular compartments. Consequently, mitochondria and peroxisomes possess a similar fraction of proteins of a-proteobacterial proteins (Gabaldon et al. 2006), whereas up to 80% of the mitochondrial proteome can be made up from proteins that have various non-a-proteobacterial origins. (Modified from Gabaldon and Huynen 2004)...

$Fig. 7.2. The vast majority of mitochondrial proteins did not originate from the ancestral a-proteobacterial endosymbiont but from a variety of eukaryotic, eubacterial, and archaeal sources (Gabaldon and Huynen 2004 Esser et al. 2004 Timmis et al. 2004). The evolution of mitochondria was not only accompanied by a substantial loss of superfluous genes, but also by the transfer of many a-proteobacterial genes into the nucleus. As a consequence, many a-proteobacterial proteins were retargeted to other cellular compartments. Consequently, mitochondria and peroxisomes possess a similar fraction of proteins of a-proteobacterial proteins (Gabaldon et al. 2006), whereas up to 80% of the mitochondrial proteome can be made up from proteins that have various non-a-proteobacterial origins. (Modified from Gabaldon and Huynen 2004)...$

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