Binding of mitochondrial ATPase from ox heart to its naturally occurring inhibitor protein: Localization by antibody binding

1983 ◽  
Vol 3 (10) ◽  
pp. 921-926 ◽  
Author(s):  
Philip J. Jackson ◽  
David A. Harris
Keyword(s):  
Binding Site ◽  
Protein Localization ◽  
Antibody Binding ◽  
Heart Mitochondria ◽  
Mitochondrial Atpase ◽  
Β Subunit ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
Naturally Occurring ◽  
The Cross

The naturally occurring ATPase inhibitor protein from ox heart mitochondria was cross-linked to its binding site on the mitochondrial ATPase using 1-ethyl-3-(dimethylamino)propyl carbodiimide. The cross-linked product, when transferred electrophoretically to a nitrocellulose sheet, reacted with antibodies directed against the inhibitor protein and the β-subunit of the ATPase. It was concluded that the binding site for the inhibitor protein lies on the β-subunit.

scholarly journals Suppression of mitochondrial ATPase inhibitor protein (IF1) in the liver of late septic rats

2007 ◽  
Vol 1767 (7) ◽  
pp. 888-896 ◽  
Author(s):  
Li-Ju Huang ◽  
Chin Hsu ◽  
Tsen-Ni Tsai ◽  
Shu-Jung Wang ◽  
Rei-Cheng Yang
Keyword(s):  
Mitochondrial Atpase ◽  
Inhibitor Protein ◽  
Atpase Inhibitor

Release of the inhibitory action of the natural ATPase inhibitor protein on the mitochondrial ATPase

1984 ◽  
Vol 144 (1) ◽  
pp. 151-157 ◽  
Author(s):  
Carmen BELTRAN ◽  
Marietta T. GOMEZ-PUYOU ◽  
Armando GOMEZ-PUYOU ◽  
Alberto DARSZON
Keyword(s):  
Inhibitory Action ◽  
Mitochondrial Atpase ◽  
Inhibitor Protein ◽  
Atpase Inhibitor

Action of the mitochondrial ATPase inhibitor protein on the Ca2+-ATPase of sarcoplasmic reticulum

1983 ◽  
Vol 111 (1) ◽  
pp. 274-279 ◽  
Author(s):  
Leopoldo de Meis ◽  
Marietta Tuena de Gómez-Puyou ◽  
Armando Gómez-Puyou
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Mitochondrial Atpase ◽  
Inhibitor Protein ◽  
Atpase Inhibitor

scholarly journals Functional domains of the ATPase inhibitor protein from bovine heart mitochondria

FEBS Letters ◽  
2000 ◽  
Vol 482 (1-2) ◽  
pp. 163-166 ◽  
Author(s):  
Franco Zanotti ◽  
Gabriella Raho ◽  
Rita Vuolo ◽  
Antonio Gaballo ◽  
Francesco Papa ◽  
...  
Keyword(s):  
Heart Mitochondria ◽  
Functional Domains ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
Bovine Heart

The ATPase Inhibitor Protein from Bovine Heart Mitochondria:  The Minimal Inhibitory Sequence†

Biochemistry ◽  
1996 ◽  
Vol 35 (49) ◽  
pp. 15618-15625 ◽  
Author(s):  
Mark J. van Raaij ◽  
George L. Orriss ◽  
Martin G. Montgomery ◽  
Michael J. Runswick ◽  
Ian M. Fearnley ◽  
...  
Keyword(s):  
Heart Mitochondria ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
Bovine Heart

scholarly journals Sites of protein-protein interaction on the mitochondrial F1-ATPase inhibitor protein

1986 ◽  
Vol 235 (2) ◽  
pp. 577-583 ◽  
Author(s):  
P J Jackson ◽  
D A Harris
Keyword(s):  
Acetic Anhydride ◽  
Protein A ◽  
Mitochondrial Atpase ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
F1 Atpase ◽  
Protein Protein Interaction ◽  
Restricted Environment ◽  
Hydrophilic Residues ◽  
A Site

We have investigated the structure of the mitochondrial F1-ATPase inhibitor protein from ox heart by using a differential trace-labelling method. This method has also been used to determine sites on the inhibitor protein involved in binding to both the isolated mitochondrial ATPase (F1) and to a specific anti-inhibitor antibody. Native, free inhibitor was trace-labelled on its lysine and serine residues with [14C]acetic anhydride, and inhibitor protein unfolded in guanidinium chloride or specifically bound to another protein, with [3H]acetic anhydride. Exposure/concealment of residues was deduced from the 14C/3H ratios of the peptides in a proteolytic digest of the inhibitor, after separation by h.p.l.c. None of the lysine or serine residues in the native inhibitor are as exposed as in the unfolded form. There is a gradient of reactivity, with residues 54-58 being most concealed and exposure increasing towards either end of the protein. A slight decrease in reactivity is noted in residues 1-3, suggesting that the N-terminus may be in a fairly restricted environment. These findings are discussed in the light of the predicted structure of the inhibitor protein. All but one of the labelled residues increases in reactivity when inhibitor protein binds to F1. The exception, Lys-24, is only slightly concealed. Hence, F1 binding appears not to involve the lysine or serine residues directly. This finding is consistent with the view that the F1-inhibitor interaction is hydrophobic in nature. Complementary information was provided using an anti-inhibitor antibody that binds to a site on the inhibitor different from that at which F1 binds. Binding of this antibody conceals residues 54, 58, and 65 considerably. This confirms that F1 does not interact with these hydrophilic residues on the inhibitor protein.

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