Regulatory proteins of F1F0-ATPase: Role of ATPase inhibitor
Authors:
- 1 February 1990
- journal article
- review article
- Published by Springer Nature in Journal of Bioenergetics and Biomembranes
- Vol. 22 (1) , 27-38
Abstract
An intrinsic ATPase inhibitor inhibits the ATP-hydrolyzing activity of mitochondrial F1F0-ATPase and is released from its binding site on the enzyme upon energization of mitochondrial membranes to allow phosphorylation of ADP. The mitochondrial activity to synthesize ATP is not influenced by the absence of the inhibitor protein. The enzyme activity to hydrolyze ATP is induced by dissipation of the membrane potential in the absence of the inhibitor. Thus, the inhibitor is not responsible for oxidative phosphorylation, but acts only to inhibit ATP hydrolysis by F1F0-ATPase upon deenergization of mitochondrial membranes. The inhibitor protein forms a regulatory complex with two stabilizing factors, 9K and 15K proteins, which facilitate the binding of the inhibitor to F1F0-ATPase and stabilize the resultant inactivated enzyme. The 9K protein, having a sequence very similar to the inhibitor, binds directly to F1 in a manner similar to the inhibitor. The 15K protein binds to the F0 part and holds the inhibitor and the 9K protein on F1F0-ATPase even when one of them is detached from the F1 part.Keywords
This publication has 65 references indexed in Scilit:
- Binding of dicyclohexylcarbodiimide to a native F1-ATPase - inhibitor protein complex isolated from bovine heart mitochondriaBiochemical and Biophysical Research Communications, 1988
- The mitochondrial ATP synthase inhibitor protein binds near the C‐terminus of the F1 β‐subunitFEBS Letters, 1988
- Complete amino‐acid sequence of the natural ATPase inhibitor from the mitochondria of the yeast Candida utilisEuropean Journal of Biochemistry, 1987
- Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondriaJournal of Molecular Biology, 1985
- Oligomycin sensitivity‐conferring protein (OSCP) of beef heart mitochondriaFEBS Letters, 1984
- Primary structure of a regulating factor, 15 kDa protein, of ATP synthase in yeast mitochondriaFEBS Letters, 1984
- ATP synthesis and hydrolysis in submitochondrial particles subjected to an acid—base transitionFEBS Letters, 1983
- Electrochemical gradient induced displacement of the natural ATPase inhibitor protein from mitochondrial ATPase as detected by antibodies against the inhibitor proteinBiochemical and Biophysical Research Communications, 1981
- Mitochondrial adenosinetriphosphatase inhibitor protein: reversible interaction with complex V (ATP synthetase complex)Biochemistry, 1981
- Radiolabeling of natural adenosine triphosphatase inhibitor with phenyl[14C]isothiocyanate and study of its interaction with mitochondrial adenosine triphosphatase. Localization of inhibitor binding sites and stoichiometry of bindingBiochemistry, 1980