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Showing papers on "Mitochondrial biogenesis published in 1981"



Journal ArticleDOI
TL;DR: There is a substantial increase in the amount and activity of the light type of mitochondria due to their de novo synthesis after imbibition, and there is synthesis of proteins comparable to that into light mitochondria during the decline.
Abstract: There are two types of mitochondria present in imbibed peanut cotyledons: a light type (density 1.182 grams per cubic centimeter) and a heavy type (density 1.205 grams per cubic centimeter). The membrane fractions from these two types can be distinguished using sucrose density gradient analysis, and differences in membrane density between the light and heavy types are reflected in differences in their protein N and phospholipid P composition. With increasing time after imbibition, there is a substantial increase in the amount and activity of the light type of mitochondria due to their de novo synthesis. The membrane density of the light mitochondrial fraction declines over 5 days after the start of imbibition as the phospholipid P to protein N ratio increases. The heavy mitochondrial fraction declines during the first 3 days after the start of imbibition, and then it remains at a low, but constant, level thereafter. Even during the decline, however, there is synthesis of proteins comparable to that into light mitochondria. The mitochondrial biogenesis that has been observed in peanut cotyledons is of the light type, the function and physiological importance of the minor heavy type is not known.

22 citations


Book ChapterDOI
TL;DR: The successful application of mutant and recombinant analysis, coupled with physical techniques including the use of restriction enzymes, has allowed the identification and mapping of many of the genes located on yeast mtDNA.
Abstract: Since the discovery that mitochondria contain DNA a considerable amount of effort has been directed towards the analysis of mitochondrial DNA (mt DNA) and its gene products. The majority of the work has been carried out with the yeast, Saccharomyces cerevisiae. although there have been important contributions from those working with Neurospora and mimal cells (see Borst and Grivell, 1978, and articles in Bandlow et al, 1977). The successful application of mutant and recombinant analysis, coupled with physical techniques including the use of restriction enzymes, has allowed the identification and mapping of many of the genes located on yeast mtDNA (Borst and Grivell, 1978; Schweyen et al, 1978, Butow and Strausberg, 1979).

19 citations


Journal ArticleDOI
TL;DR: In this article, it was shown that a mitochondrial translation product (M r, 32 000) previously thought to be a subunit of the membrane sector of the yeast mitochondrial ATPase is a contaminant, consisting of subunit II of the cytochrome oxidase complex and cyto-chrome b apoprotein.

18 citations



Journal ArticleDOI
TL;DR: The increase in the cytochrome concentration in the intestinal cells of the hypoxic rats must be due to the longer life of the cells, which allows for the synthesis of larger amounts of the mitochondrial components.
Abstract: The effects of hypoxia in vivo (40.8 kPa barometric pressure up to 120 h) and fasting on the characteristics of intestinal epithelial villous cell mitochondria and the turnover of epithelial villous cells and mitochondria were studied in rats. Using cells and mitochondria isolated in the isotonic mannitol medium, it was found that 24-h hypoxia or fasting did not alter the mitochondrial cytochrome content, but 48-h hypoxia or fasting led to increases of 70% and 37% in the cytochrome aa3 concentration in the hypoxic and fasting animals respectively. The turnover of intestinal epithelial cells was studied by observing the labelling kinetics of the cells with 3H-thymidine and the turnover of the cell and mitochondrial proteins with (guanido-14C)-arginine or 3H-leucine. The decay in thymidine radioactivity obeyed exponential kinetics from which half-lives of 1.15, 1.31 and 1.53 days were calculated in the control, fasting and hypoxic animals respectively. The half-lives for total cellular protein were 1.31, 1.54 and 1.54 days respectively when calculated from the (guanido-14C)-arginine experiments, or 0.69, 0.75 and 0.99 days when calculated from the leucine experiments. The labelling experiments with (guanido-14C)-arginine indicated that the turnover of mitochondrial proteins in intestinal epithelial cells is the same as that of the cells themselves. Since the turnover of mitochondrial proteins in other tissues is shown to be a relatively slow process, the increase in the cytochrome concentration in the intestinal cells of the hypoxic rats must be due to the longer life of the cells, which allows for the synthesis of larger amounts of the mitochondrial components.

3 citations


Journal ArticleDOI
TL;DR: Two-dimensional electrophoretic analysis of the mitochondrial translation products of four mit-mutants indicate that subunit III of cytochrome oxidase is the only mitochondrial translation product affected by mutations in the oxi2 region of the mtDNA.

3 citations