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Andersson, S. G. E.; Karlberg, O.; Canbäck, B.; Kurland, C. G. (2003): On the origin of mitochondria: a genomics perspective. In: Philos. Trans. R. Soc. Lond. B. Biol. Sci.. 358 , 165-179
Titel des Artikels
On the origin of mitochondria: a genomics perspective
The availability of complete genome sequence data from both bacteria and eukaryotes provides information about the contribution of bacterial genes to the origin and evolution of mitochondria. Phylogenetic analyses based on genes located in the mitochondrial genome indicate that these genes originated from within the alpha-proteobacteria. A number of ancestral bacterial genes have also been transferred from the mitochondrial to the nuclear genome, as evidenced by the presence of orthologous genes in the mitochondrial genome in some species and in the nuclear genome of other species. However, a multitude of mitochondrial proteins encoded in the nucleus display no homology to bacterial proteins, indicating that these originated within the eukaryotic cell subsequent to the acquisition of the endosymbiont. An analysis of the expression patterns of yeast nuclear genes coding for mitochondrial proteins has shown that genes predicted to be of eukaryotic origin are mainly translated on polysomes that are free in the cytosol whereas those of putative bacterial origin are translated on polysomes attached to the mitochondrion. The strong relationship with alpha-proteobacterial genes observed for some mitochondrial genes, combined with the lack of such a relationship for others, indicates that the modern mitochondrial proteome is the product of both reductive and expansive processes.
Appaix, F.; Kuznetsov, A. V.; Usson, Y.; Kay, L.; Andrienko, T.; Olivares, J.; Kaambre, T.; Sikk, P.; Margreiter, R.; Saks, V. (2003): Possible role of cytoskeleton in intracellular arrangement and regulation of mitochondria. In: Exp. Physiol.. 88 , 175-190
Bay, D. C.; Court, D. A. (2002): Origami in the outer membrane: the transmembrane arrangement of mitochondrial porins. In: Biochem. Cell Biol.. 80 , 551-562
Carr, H. S.; Winge, D. R. (2003): Assembly of cytochrome c oxidase within the mitochondrion. In: Acc. Chem. Res.. 36 , 309-316
Chinnery, P. F.; Schon, E. A. (2003): Mitochondria. In: J. Neurol. Neurosurg. Psychiatry. 74 , 1188-1199
Collins, T. J.; Bootman, M. D. (2003): Mitochondria are morphologically heterogeneous within cells. In: J. Exp. Biol.. 206 , 1993-2000
Das, A. M. (2003): Regulation of the mitochondrial ATP-synthase in health and disease. In: Mol. Genet. Metab.. 79 , 71-82
Eckert, A.; Keil, U.; Kressmann, S.; Schindowski, K.; Leutner, S.; Leutz, S.; Müller, W. E. (2003): Effects of EGb 761 Ginkgo biloba extract on mitochondrial function and oxidative stress. In: Pharmacopsychiatry. 36 , S15-S23
Embley, T. M.; van der Giezen, M.; Horner, D. S.; Dyal, P. L.; Foster, P. (2003): Mitochondria and hydrogenosomes are two forms of the same fundamental organelle. In: Philos. Trans. R. Soc. Lond. B. Biol. Sci.. 358 , 191-202
Genova, M. L.; Bianchi, C.; Lenaz, G. (2003): Structural organization of the mitochondrial respiratory chain. In: Ital. J. Biochem.. 52 , 58-61
Heazlewood, J. L.; Millar, A. H.; Day, D. A.; Whelan, J. (2003): What makes a mitochondrion?. In: Genome Biol.. 4 , 218
Karlberg, E. O. L.; Andersson, S. G. E. (2003): Mitochondrial gene history and mRNA localization: is there a correlation?. In: Nat. Rev. Genet.. 4 , 391-397
Ly, J. D.; Grubb, D. R.; Lawen, A. (2003): The mitochondrial membrane potential (Δψm) in apoptosis; an update. In: Apoptosis. 8 (2) , 115-128
Titel des Artikels
The mitochondrial membrane potential (Δψm) in apoptosis; an update
Mitochondrial dysfunction has been shown to participate in the induction of apoptosis and has even been suggested to be central to the apoptotic pathway. Indeed, opening of the mitochondrial permeability transition pore has been demonstrated to induce depolarization of the transmembrane potential (Δψm), release of apoptogenic factors and loss of oxidative phosphorylation. In some apoptotic systems, loss of Δψm may be an early event in the apoptotic process. However, there are emerging data suggesting that, depending on the model of apoptosis, the loss of Δψm may not be an early requirement for apoptosis, but on the contrary may be a consequence of the apoptotic-signaling pathway. Furthermore, to add to these conflicting data, loss of Δψm has been demonstrated to not be required for cytochrome c release, whereas release of apoptosis inducing factor AIF is dependent upon disruption of Δψm early in the apoptotic pathway. Together, the existing literature suggests that depending on the cell system under investigation and the apoptotic stimuli used, dissipation of Δψm may or may not be an early event in the apoptotic pathway. Discrepancies in this area of apoptosis research may be attributed to the fluorochromes used to detect Δψm. Differential degrees of sensitivity of these fluorochromes exist, and there are also important factors that contribute to their ability to accurately discriminate changes in Δψm.
Miyagishima, S.; Nishida, K.; Kuroiwa, T. (2003): An evolutionary puzzle: chloroplast and mitochondrial division rings. In: Trends Plant Sci.. 8 , 432-438
Newmeyer, D. D.; Ferguson-Miller, S. (2003): Mitochondria: releasing power for life and unleashing the machineries of death. In: Cell. 112 , 481-490
Nisoli, E.; Clementi, E.; Moncada, S.; Carruba, M. O. (2004): Mitochondrial biogenesis as a cellular signaling framework. In: Biochem. Pharmacol.. 67 , 1-15
Ohta, S. (2003): A multi-functional organelle mitochondrion is involved in cell death, proliferation and disease. In: Curr. Med. Chem.. 10 , 2485-2494
Osteryoung, K. W.; Nunnari, J. (2003): The division of endosymbiotic organelles. In: Science. 302 , 1698-1704
Punj, V.; Chakrabarty, A. M. (2003): Redox proteins in mammalian cell death: an evolutionarily conserved function in mitochondria and prokaryotes. In: Cell Microbiol.. 5 , 225-231
Richter, O. H.; Ludwig, B. (2003): Cytochrome c oxidase - structure, function, and physiology of a redox-driven molecular machine. In: Rev. Physiol. Biochem. Pharmacol.. 147 , 47-7410.1007/s10254-003-0006-0
Titel des Artikels
Cytochrome c oxidase - structure, function, and physiology of a redox-driven molecular machine
Cytochome c oxidase is the terminal member of the electron transport chains of mitochondria and many bacteria. Providing an efficient mechanism for dioxygen reduction on the one hand, it also acts as a redox-linked proton pump, coupling the free energy of water formation to the generation of a transmembrane electrochemical gradient to eventually drive ATP synthesis. The overall complexity of the mitochondrial enzyme is also reflected by its subunit structure and assembly pathway, whereas the diversity of the bacterial enzymes has fostered the notion of a large family of heme-copper terminal oxidases. Moreover, the successful elucidation of 3-D structures for both the mitochondrial and several bacterial oxidases has greatly helped in designing mutagenesis approaches to study functional aspects in these enzymes.
Schon, E. A.; DiMauro, S. (2003): Medicinal and genetic approaches to the treatment of mitochondrial disease. In: Curr. Med. Chem.. 10 , 2523-2533
Searcy, D. G. (2003): Metabolic integration during the evolutionary origin of mitochondria. In: Cell Res.. 13 , 229-238
Tielens, A. G. M.; Rotte, C.; van Hellemond, J. J.; Martin, W. (2002): Mitochondria as we don't know them. In: Trends Biochem. Sci.. 27 , 564-572
Turcotte, L. P. (2003): Mitochondria: biogenesis, structure, and function - symposium introduction. In: Med. Sci. Sports Exerc.. 35 , 82-85
van Hellemond, J. J.; van der Klei, A.; van Weelden, S. W. H.; Tielens, A. G. M. (2003): Biochemical and evolutionary aspects of anaerobically functioning mitochondria. In: Philos. Trans. R. Soc. Lond. B. Biol. Sci.. 358 , 205-21510.1098/rstb.2002.1182
Titel des Artikels
Biochemical and evolutionary aspects of anaerobically functioning mitochondria
Mitochondria are usually considered to be the powerhouses of the cell and to be responsible for the aerobic production of ATP. However, many eukaryotic organisms are known to possess anaerobically functioning mitochondria, which differ significantly from classical aerobically functioning mitochondria. Recently, functional and phylogenetic studies on some enzymes involved clearly indicated an unexpected evolutionary relationship between these anaerobically functioning mitochondria and the classical aerobic type. Mitochondria evolved by an endosymbiotic event between an anaerobically functioning archaebacterial host and an aerobic alpha-proteobacterium. However, true anaerobically functioning mitochondria, such as found in parasitic helminths and some lower marine organisms, most likely did not originate directly from the pluripotent ancestral mitochondrion, but arose later in evolution from the aerobic type of mitochondria after these were already adapted to an aerobic way of life by losing their anaerobic capacities. This review will focus on some biochemical and evolutionary aspects of these fermentative mitochondria, with special attention to fumarate reductase, the synthesis of the rhodoquinone involved, and the enzymes involved in acetate production (acetate : succinate CoA-transferase and succinyl CoA-synthetase).

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