Protein synthesis by isolated pea mitochondria is dependent on the activity of respiratory complex II

In isolated pea (Pisum sativum L.) mitochondria incorporation of S-35-methionine into newly synthesised proteins was influenced by the presence of site-specific inhibitors of the respiratory electron-transport chain. These effects were not produced by changes in the rate of respiratory electron transport itself nor by changes in ATP concentration. Protein synthesis was inhibited by inhibitors of ubiquinone reduction but not by inhibitors of ubiquinol oxidation. By the use of additional inhibitors at specific sites of the respiratory chain, different oxidation-reduction states were obtained for the different complexes in the electron-transport chain. It was found that electron transport through succinate:ubiquinone oxidoreductase (respiratory complex II) was specifically required for protein synthesis, even when all the other conditions for protein synthesis were satisfied. We suggest that a subunit of complex II, or a component closely associated with complex II, is involved in a regulatory system that couples electron transport to protein synthesis.