Lack of ability of trypsin-treated mitochondrial F1-ATPase to bind the oligomycin-sensitivity conferring protein (OSCP).
Soluble beef-heart mitochondrial F1-ATPase modified in its alpha-subunit by mild trypsin treatment (alpha'-F1) can no longer bind oligomycin-sensitivity conferring protein (OSCP) but is still capable of binding to F1-depleted submitochondrial particles, giving rise to a maximally oligomycin-sensitive ATPase, provided the particles contain their native complement of OSCP. When OSCP is removed from the particles, alpha'-F1 can still bind to the particles, but added OSCP induces only a low degree of oligomycin sensitivity. The possible role of OSCP in the functional coupling of the catalytic (F1) and H+-translocating (Fo) moieties of mitochondrial ATPase is discussed. The results suggest a functional similarity between the OSCP component of mitochondrial ATPase and the delta-subunit of E. coli ATPase, which is in accordance with the structural homology recently found to exist between the two polypeptides.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000641:Ammonia / Q000494:pharmacology; D000818:Animals; D002352:Carrier Proteins; D002417:Cattle; D004492:Edetic Acid / Q000494:pharmacology; D008565:Membrane Proteins / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000187:drug effects / Q000201:enzymology*; D025261:Mitochondrial Proton-Translocating ATPases; D009840:Oligomycins / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013367:Submitochondrial Particles / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology*
D002352:Carrier Proteins; D008565:Membrane Proteins; D009840:Oligomycins; D000641:Ammonia; D004492:Edetic Acid; D014357:Trypsin; D000251:Adenosine Triphosphatases; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases; C020439:oligomycin sensitivity-conferring protein