Molecular and Cellular Biochemistry

, Volume 14, Issue 1–3, pp 109–113 | Cite as

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

  • Ya. M. Rabinovitz
  • H. A. Pinus
  • A. V. Kotelnikova
Article

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.

Keywords

Protein Synthesis Inhibitory Action Leucine Mitochondrial Membrane Oxidative Phosphorylation 

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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Copyright information

© Dr. W. Junk b.v. Publishers 1977

Authors and Affiliations

  • Ya. M. Rabinovitz
    • 1
  • H. A. Pinus
    • 1
  • A. V. Kotelnikova
    • 1
  1. 1.Bakh Institute of BiochemistryAcademy of SciencesMoscowUSSR

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