The biogenesis of rat-liver mitochondrial ATPase. Evidence that the N, N'-dicyclohexyl carbodiimide-binding protein is synthesized outside the mitochondria.
1. Radioactive N,N'-dicyclohexyl carbodiimide (DCCD) is bound as effectively to the N, N'-dicyclohexyl carbodiimide- and oligomycin-sensitive ATPase complex in submitochondrial particles of normal rat liver as to the similar but partially N,N'-dicyclohexyl carbodiimide- and oligomycin-insensitive complex of thiamphenicol-treated rats. The latter complex is deficient in 3 subunits (subunit 6, 7 and 10). 2. Radioactive N,N'-dicyclohexyl carbodiimide is exclusively bound to the subunits present in the bands 8 and 11 of SDS-PAA gels of the purified ATPase complex. These subunits, most likely the dimer and monomer of the N,N'-dicyclohexyl carbodiimide-binding protein, are products of the cytoplasmic protein synthesis. 3. The results together indicate that the N,N'-dicyclohexyl carbodiimide-insensitivity of the ATPase complex formed during in vitro inhibition of mitochondrial protein synthesis, is not caused by a lack of inhibitor binding protein. The same holds for the oligomycin-insensitivity.
D000251:Adenosine Triphosphatases / Q000096:biosynthesis*; D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D004024:Dicyclohexylcarbodiimide / Q000378:metabolism; D008297:Male; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology*; D009840:Oligomycins / Q000494:pharmacology; D011485:Protein Binding; D051381:Rats; D013367:Submitochondrial Particles / Q000378:metabolism; D013839:Thiamphenicol / Q000494:pharmacology
D002352:Carrier Proteins; D009840:Oligomycins; D004024:Dicyclohexylcarbodiimide; D000251:Adenosine Triphosphatases; D013839:Thiamphenicol