Recombinant bovine heart mitochondrial F1-ATPase inhibitor protein: Overproduction in Escherichia coli, purification, and structural studies

Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 10140-10149 ◽  
Author(s):  
Gino Van Heeke ◽  
Lily Deforce ◽  
Richard A. Schnizer ◽  
Regina Shaw ◽  
Judy M. Couton ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Studies ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
F1 Atpase ◽  
Bovine Heart ◽  
Protein Overproduction

scholarly journals The adenosine triphosphatase-inhibitor content of bovine heart submitochondrial particles. Influence of the inhibitor on adenosine triphosphate-dependent reactions

1977 ◽  
Vol 162 (2) ◽  
pp. 351-357 ◽  
Author(s):  
S J Ferguson ◽  
D A Harris ◽  
G K Radda
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Type I ◽  
Type Ii ◽  
Inhibitor Protein ◽  
Isolation Method ◽  
Atpase Inhibitor ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Tightly Bound Nucleotides

1. The activity of the ATPase (adenosine triphosphatase) of phosphorylating particles prepared by sonication of bovine heart mitochondria in the presence of MgCl2 and ATP is influenced by the isolation method for the mitochondria used in the preparation of particles. Type-I particles, made from mitochondria isolated in a medium lacking succinate, have a lower ATPase activity than to Type-II particles, which are prepared from mitochondria isolated in a medium containing succinate. 2. Centrifugation under appropriate energized conditions increases the ATPase activity of Type-I particles almost to that of the Type-II particles. The ATPase activity of Type-II particles was only slightly stimulated by this procedure. These data are interpreted as indicating a higher content of the ATPase-inhibitor protein in the Type-I particles. 3. A comparison was made of the ATP-driven enhancement of 8-anilinonaphthalene-1-sulphonate fluorescence and the exchange of the endogenous tightly bound nucleotides of the ATPase in Type-I and Type-II particles. The effect of exogenous inhibitor protein on both these reactions was also studied. 4. The time-scale on which the inhibitor protein can exchange between ATPase molecules is discussed.

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 Modulation of the Oligomerization State of the Bovine F1-ATPase Inhibitor Protein, IF1, by pH

2000 ◽  
Vol 275 (33) ◽  
pp. 25460-25464 ◽  
Author(s):  
Elena Cabezon ◽  
P. Jonathan G. Butler ◽  
Michael J. Runswick ◽  
John E. Walker
Keyword(s):  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
F1 Atpase

Inhibitors of the catalytic domain of mitochondrial ATP synthase

2006 ◽  
Vol 34 (5) ◽  
pp. 989-992 ◽  
Author(s):  
J.R. Gledhill ◽  
J.E. Walker
Keyword(s):  
Atp Synthase ◽  
Binding Sites ◽  
Catalytic Domain ◽  
Structural Studies ◽  
Inhibitor Protein ◽  
X Ray ◽  
F1 Atpase ◽  
X Ray Crystallography ◽  
Mitochondrial Atp Synthase ◽  
Natural Inhibitor

An understanding of the mechanism of ATP synthase requires an explanation of how inhibitors act. The catalytic F1-ATPase domain of the enzyme has been studied extensively by X-ray crystallography in a variety of inhibited states. Four independent inhibitory sites have been identified by high-resolution structural studies. They are the catalytic site, and the binding sites for the antibiotics aurovertin and efrapeptin and for the natural inhibitor protein, IF1.

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.

Peptide analogs of the beef heart mitochondrial F1-ATPase inhibitor protein

Biochemistry ◽  
1993 ◽  
Vol 32 (29) ◽  
pp. 7496-7502 ◽  
Author(s):  
Jay S. Stout ◽  
Bruce E. Partridge ◽  
Donald A. Dibbern ◽  
Sheldon M. Schuster
Keyword(s):  
Beef Heart ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
F1 Atpase ◽  
Peptide Analogs
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