Characterization of the phosphoenolpyruvate inhibition of mitochondrial protein synthesis.

The interaction of phosphoenolypyruvate with isolated rat liver mitochondria has been further investigated. The uptake of P-enolpyruvate is accompanied by the stoichiometric release of intramitochondrial adenine nucleotides resulting in the inhibition of mitochondrial protein synthesis. Addition of specific inhibitors of either the adenine nucleotide carrier or the tricarboylic acid carrier blocks the P-enolpyruvate-stimulated loss of adenine nucleotides and thereby prevents the resultant inhibition of mitochondrial protein synthesis. These data suggest that there is a specific interaction between the mitochondrial adenine nucleotide translocase and the tricarboxylic acid carrier resulting in the control of intramitochondrial adenine nucleotide levels of phosphoenolpyruvate.