Specific inhibition of mitochondrial protein synthesis influences the amount of complex I in mitochondria of rat liver and Neurospora crassa directly.
Specific inhibition of mitochondrial protein synthesis reduces the oxidation rate of NADH-linked substrates in rat liver as well as in Neurospora crassa mitochondria. The present study shows that this is due to the fact that inhibition of mitochondrial protein synthesis leads to a decrease of the concentration of active complex I. Therefore, these results demonstrate that at least one of the genes for the subunits of complex I is localized on mitochondrial DNA.
D000818:Animals; D002701:Chloramphenicol / Q000494:pharmacology*; D003580:Cytochromes / Q000096:biosynthesis / Q000235:genetics; D004272:DNA, Mitochondrial / Q000235:genetics; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008928:Mitochondria / Q000187:drug effects / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology*; D016660:NAD(P)H Dehydrogenase (Quinone); D010118:Oxytetracycline / Q000494:pharmacology*; D014176:Protein Biosynthesis / Q000187:drug effects*; D011725:Pyridines / Q000494:pharmacology; D011808:Quinone Reductases / Q000096:biosynthesis* / Q000235:genetics; D051381:Rats; D011919:Rats, Inbred Strains
D003580:Cytochromes; D004272:DNA, Mitochondrial; D011725:Pyridines; D002701:Chloramphenicol; C100213:piericidin A; D016660:NAD(P)H Dehydrogenase (Quinone); D011808:Quinone Reductases; D010118:Oxytetracycline