The oligomycin axis of mitochondrial ATP synthase: OSCP and the proton channel

• Published in: Journal of bioenergetics and biomembranes Vol. 32; no. 5; pp. 507 - 515
• Main Authors: Devenish, R J, Prescott, M, Boyle, G M, Nagley, P
• Format: Journal Article
• Language: English
• Published: United States Springer Nature B.V 01.10.2000
• Subjects: Adenosine triphosphatase; Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; Animals; ATP; Binding Sites; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - metabolism; Enzymes; Membrane Proteins - chemistry; Membrane Proteins - genetics; Membrane Proteins - metabolism; Mitochondrial Proton-Translocating ATPases - antagonists & inhibitors; Mitochondrial Proton-Translocating ATPases - chemistry; Mitochondrial Proton-Translocating ATPases - metabolism; Models, Molecular; Multiprotein Complexes; Oligomycins - pharmacology; Protein Subunits; Proteins; Rats; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Saccharomyces cerevisiae - enzymology
• ISSN: 0145-479X; 1573-6881
• DOI: 10.1023/A:1005621125812

Oligomycin has long been known as an inhibitor of mitochondrial ATP synthase, putatively binding the F(o) subunits 9 and 6 that contribute to proton channel function of the complex. As its name implies, OSCP is the oligomycin sensitivity-conferring protein necessary for the intact enzyme complex to display sensitivity to oligomycin. Recent advances concerning the structure and mechanism of mitochondrial ATP synthase have led to OSCP now being considered a component of the peripheral stator stalk rather than a central stalk component. How OSCP confers oligomycin sensitivity on the enzyme is unknown, but probably reflects important protein-protein interactions made within the assembled complex and transmitted down the stator stalk, thereby influencing proton channel function. We review here our studies directed toward establishing the stoichiometry, assembly, and function of OSCP in the context of knowledge of the organization of the stator stalk and the proton channel.