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

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

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.

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 frayed N-terminal of the inhibitor protein of bovine mitochondrial F1-ATPase

1986 ◽  
Vol 235 (2) ◽  
pp. 515-519 ◽  
Author(s):  
M J Runswick ◽  
J E Walker ◽  
B W Gibson ◽  
D H Williams
Keyword(s):  
Glutamic Acid ◽  
Terminal Region ◽  
Proteolytic Processing ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
F1 Atpase

The N-terminal region of the bovine mitochondrial F1-ATPase inhibitor protein is frayed. In three independently isolated samples about 62% of chains start at glycine-1. A further 22% of chains start at residue 2, serine, and the remainder at residue 3, glutamic acid. No evidence can be found for alpha-N-formylglycine reported previously. The fraying may be a consequence of proteolytic processing of the precursor of the inhibitor protein during entry into the mitochondrion.

The interaction of mitochondrial F1-ATPase with the natural ATPase inhibitor protein

1980 ◽  
Vol 592 (3) ◽  
pp. 385-395 ◽  
Author(s):  
M.Tuena De Gómez-Puyou ◽  
K. Nordenbrand ◽  
U. Muller ◽  
A. Gómez-Puyou ◽  
Lars Ernster
Keyword(s):  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
F1 Atpase
Sign in / Sign up

Export Citation Format

Share Document