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Relationship of protein synthesis and energetics in mitochondria

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Abstract

Protein synthesis in rat liver mitochondria has been studied by measuring14C-leucine incorporation into mitochondrial proteins. It has been found that addition of uncouplers of oxidative phosphorylation or cyanide inhibits leucine incorporation supported by ATP energy in the presence of oligomycin. Neither cyanide nor oligomycin used separately suppresses the ATP-supported leucine incorporation. Oligomycin arrests respiration-supported protein synthesis. These facts indicate that both ATP and membrane potential or another form of non-phosphorylated energized state are necessary for the use of extramitochondrial amino acids for protein synthesis in mitochondria.

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Authors and Affiliations

  1. Bakh Institute of Biochemistry, USSR Academy of Sciences, USSR

    S. A. Mityagina, H. A. Pinus, Ya. M. Rabinowitz & V. P. Skulachev

  2. Department of Bioenergetics, Laboratory of Bioorganic Chemistry, Moscow State University, USSR

    S. A. Mityagina, H. A. Pinus, Ya. M. Rabinowitz & V. P. Skulachev

Authors
  1. S. A. Mityagina
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  2. H. A. Pinus
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  3. Ya. M. Rabinowitz
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  4. V. P. Skulachev
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Mityagina, S.A., Pinus, H.A., Rabinowitz, Y.M. et al. Relationship of protein synthesis and energetics in mitochondria. J Bioenerg Biomembr 3, 399–402 (1972). https://doi.org/10.1007/BF01516078

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  • DOI: https://doi.org/10.1007/BF01516078

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