Temperature-dependency of electron-transport activity in mitochondria with exogenous mitochondrial DNA in Drosophila.
In mitochondrial DNA (mtDNA) heteroplasmy induced artificially in Drosophila melanogaster (Matsuura et al., 1989), foreign mtDNA derived from D. mauritiana was selectively transmitted at 25 degrees C but was lost at 19 degrees C (Niki et al., 1989; Matsuura et al., 1990, 1991). To investigate temperature-dependent factors in the selective transmission of mtDNA, the temperature-dependency of electron-transport activity of mitochondria from D. melanogaster in which endogenous mtDNA was completely replaced by the foreign mtDNA was compared with that of D. melanogaster and D. mauritiana. For NADH-oxidase activity, the optimum temperature of D. mauritiana mitochondria was 35 degrees C while for two types of mitochondria from D. melanogaster each possessing either endogenous or exogenous mtDNA, maximum activity was noted at 32 degrees C. This observation suggests that the temperature-dependency of mitochondrial electron-transport activity is mainly determined by a nuclear genome. NADH-cytochrome c reductase and cytochrome c oxidase activities were not significantly different among the three types of mitochondria. The temperature-dependency of mitochondrial function apparently is not involved in the temperature-dependent selective transmission of mtDNA in the heteroplasmic state.
Nagata
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Department of Biology, Ochanomizu University, Tokyo, Japan.
Matsuura
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D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism; D004272:DNA, Mitochondrial / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism* / Q000648:ultrastructure; D004579:Electron Transport; D008928:Mitochondria / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D013696:Temperature
D003574:Cytochrome c Group; D004272:DNA, Mitochondrial; D009097:Multienzyme Complexes; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases