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A study of dependence of protein synthesis in mitochondria on the transmembrane potential

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Summary

1. Incorporation of [H3]leucine into the TCA insoluble fraction of rat liver mitochondria incubatedin vitro is inhibited by uncouplers of oxidative phosphorylation. The inhibition is not correlated with the activation of mitochondrial ATPase. 2. Dependence of mitochondrial protein synthesis on the transmembrane potential is manifested in a wide range of K+ and Mg++ concentrations in the incubation media. 3. The inhibitory action of uncouplers shows a lag period equal to 5–7 minutes, this lag period however is not observed when the uncoupler is added to puromycin-treated mitochondria. 4. Dependence of mitochondrial protein synthesis on the transmembrane potential, which represents a property characteristic for the inner mitochondrial membrane suggests that mitochondrial ribosomes act in close contact with the mitochondrial membrane system.

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Abbreviations

MPS:

mitochondrial protein synthesis

CAP:

chloramphenical

CCP:

2,4,6-chlorocarbonyl cyanide phenylhydrazone

FCCP:

p-trifluoromethoxy carbonyl cyanide phenylhydrazone

PEP:

phosphoenolpyruvate

Pi:

inorganic phosphate

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Authors and Affiliations

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

    Ya. M. Rabinovitz, H. A. Pinus & A. V. Kotelnikova

Authors
  1. Ya. M. Rabinovitz
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  2. H. A. Pinus
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  3. A. V. Kotelnikova
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Rabinovitz, Y.M., Pinus, H.A. & Kotelnikova, A.V. A study of dependence of protein synthesis in mitochondria on the transmembrane potential. Mol Cell Biochem 14, 109–113 (1977). https://doi.org/10.1007/BF01734173

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  • DOI: https://doi.org/10.1007/BF01734173

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