Topography of oligomycin sensitivity conferring protein in the mitochondrial adenosine triphosphatase-ATP synthase

Biochemistry ◽  
1986 ◽  
Vol 25 (11) ◽  
pp. 3397-3404 ◽  
Author(s):  
Philippe Archinard ◽  
Catherine Godinot ◽  
Jane Comte ◽  
Daniele C. Gautheron
Keyword(s):  
Atp Synthase ◽  
Adenosine Triphosphatase ◽  
Oligomycin Sensitivity Conferring Protein

Studies on the mitochondrial adenosine triphosphatase system. VI. Coupling activity of F1 subunits

1970 ◽  
Vol 48 (9) ◽  
pp. 1079-1081 ◽  
Author(s):  
David H. MacLennan ◽  
Carlton W. Paulson
Keyword(s):  
Adenosine Triphosphatase ◽  
Coupling Factor ◽  
Submitochondrial Particles ◽  
Factor I ◽  
Oligomycin Sensitivity Conferring Protein

In the presence of subsaturating levels of coupling factor I (F1 and saturating levels of the oligomycin-sensitivity-conferring protein (OSCP), the addition of subunits of F1 enhanced the rate of ATP-32Pi exchange, the rate of ATP-energized DPN+ reduction by succinate, and P/O ratios in submitochondrial particles prepared by ammonium extraction (A particles). It is postulated that a limited number of ultrastructural lesions in A particles results in uncoupling. The reconstitution of A particles by the different coupling proteins could result from the repair of several types of lesions in the membrane.

scholarly journals Studies of energy-linked reactions. Net synthesis of adenosine triphosphate by isolated adenosine triphosphate synthase preparations: a role for lipoic acid and unsaturated fatty acids

1976 ◽  
Vol 160 (3) ◽  
pp. 809-812 ◽  
Author(s):  
D E Griffiths
Keyword(s):  
Fatty Acids ◽  
Oleic Acid ◽  
Oxidative Phosphorylation ◽  
Adenosine Triphosphate ◽  
Atp Synthase ◽  
Lipoic Acid ◽  
Adenosine Triphosphatase ◽  
Unsaturated Fatty Acids ◽  
Atp Synthesis ◽  
Substrate Level

ATP synthase preparations [complex V, proton-translocatin ATPase (adenosine triphosphatase) and oligomycin-sensitive ATPase] contain stoicheiometric amounts of lipoic acid residues (up to 6mol of lipoic acid/mol of ATPase complex) and catalyse net ATP synthesis in an uncoupler-and oligomycin-sensitive reaction utilizing dihydrolipoate, oleoyl-CoA and oleic acid, or in a reaction utilizing oleoyl-S-lipoate. The terminal reactions of oxidative phosphorylation are thus analogous to those of substrate-level phosphorylation.

scholarly journals TRAP1 and cyclophilin D compete at OSCP subunit to regulate enzymatic activity and permeability transition pore opening by F-ATP synthase

2021 ◽  
Author(s):  
Giuseppe Cannino ◽  
Andrea Urbani ◽  
Marco Gaspari ◽  
Mariaconcetta Varano ◽  
Alessandro Negro ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Inhibitory Effect ◽  
Cyclophilin D ◽  
Electrophysiological Measurements ◽  
Permeability Transition Pore Opening ◽  
Pore Opening ◽  
Client Proteins ◽  
Oligomycin Sensitivity Conferring Protein

AbstractBinding of the mitochondrial chaperone TRAP1 to client proteins shapes cell bioenergetic and proteostatic adaptations, but the panel of TRAP1 clients is only partially defined. Here we show that TRAP1 interacts with F-ATP synthase, the protein complex that provides most cellular ATP. TRAP1 competes with the peptidyl-prolyl cis-trans isomerase cyclophilin D (CyPD) for binding to the oligomycin sensitivity-conferring protein (OSCP) subunit of F-ATP synthase, increasing its catalytic activity and counteracting the inhibitory effect of CyPD. Moreover, TRAP1 inhibits opening of the permeability transition pore (PTP) formed by F-ATP synthase and effectively antagonizes the PTP-inducing effect of CyPD, which elicits mitochondrial depolarization and cell death. Consistently, electrophysiological measurements indicate that TRAP1 and CyPD compete in the modulation of channel activity of purified F-ATP synthase, resulting in PTP inhibition and activation, respectively, and outcompeting each other effect on the channel. Moreover, TRAP1 counteracts PTP induction by CyPD, whereas CyPD reverses TRAP1-mediated PTP inhibition. Our data identify TRAP1 as a F-ATP synthase regulator that can influence cell bioenergetics and survival and can be targeted in pathological conditions where these processes are dysregulated, such as cancer.

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