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

• Published in: Molecular and cellular biochemistry Vol. 14; no. 1-3; p. 109
• Main Authors: Rabinovitz, Y M, Pinus, H A, Kotelnikova, A V
• Format: Journal Article
• Language: English
• Published: Netherlands 04.02.1977
• Subjects: Adenosine Triphosphatases - metabolism; Animals; Antibiotics, Antineoplastic - pharmacology; Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone - pharmacology; Chloramphenicol - pharmacology; Cycloheximide - pharmacology; Dactinomycin - pharmacology; Ethidium - pharmacology; Kinetics; Membrane Potentials - drug effects; Membranes - drug effects; Membranes - physiology; Mitochondria, Liver - drug effects; Mitochondria, Liver - metabolism; Mitochondria, Liver - physiology; Oligomycins - pharmacology; Protein Biosynthesis - drug effects; Puromycin - pharmacology; Rats
• ISSN: 0300-8177
• DOI: 10.1007/BF01734173

1. Incorporation of [H3]leucine into the TCA insoluble fraction of rat liver mitochondria incubated in 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.