Dimerization of Bovine F1-ATPase by Binding the Inhibitor Protein, IF1 *

@article{Cabezon2000DimerizationOB,
  title={Dimerization of Bovine F1-ATPase by Binding the Inhibitor Protein, IF1 *},
  author={Elena Cabezon and Ignacio Arechaga and P Jonathan and Gary Butler and J. E. Walker},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={28353 - 28355}
}
In mitochondria, the hydrolytic activity of ATP synthase is regulated by a natural inhibitor protein, IF1. The binding of IF1 to ATP synthase depends on pH values, and below neutrality, IF1 forms a stable complex with the enzyme. Bovine IF1 has two oligomeric states, dimer and tetramer, depending on pH values. At pH 6.5, where it is active, IF1 dimerizes by formation of an antiparallel α-helical coiled-coil in its C-terminal region. This arrangement places the inhibitory N-terminal regions in… 
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The structure of bovine F1-ATPase in complex with its regulatory protein IF1
TLDR
In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1, which implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.
The structure of bovine IF1, the regulatory subunit of mitochondrial F‐ATPase
TLDR
Tetramer formation masks the inhibitory region of IF1, preventing IF1 binding to ATP synthase in mitochondria.
Dimerization of F0F1ATP synthase from bovine heart is independent from the binding of the inhibitor protein IF1.
The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1
TLDR
The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF1 has been determined and provides further evidence of sequential product release, with the phosphate and the magnesium ion released before the ADP molecule.
Binding of the Inhibitor Protein IF1 to Bovine F1-ATPase
Formation of the Yeast F1F0-ATP Synthase Dimeric Complex Does Not Require the ATPase Inhibitor Protein, Inh1*
TLDR
It is concluded that dimerization of the F1F0-ATP synthase complexes involves a physical interaction of the membrane-embedded F0 sectors from two monomeric complexes and in a manner that is independent of inhibitory activity of the Inh1 and accessory proteins.
A hinge of the endogeneous ATP synthase inhibitor protein: The link between inhibitory and anchoring domains
TLDR
The data suggest that the hinge and the dimerization domain of the inhibitor protein from bovine heart are related to its ability to form stable dimers and to interact with other subunits of the ATP synthase.
Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.
TLDR
The solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence is presented, which forms an anti-parallel coiled-coil in which three of the five histidine residue occupy key positions at the dimer interface.
Kinetic analysis of the inhibition mechanism of bovine mitochondrial F1-ATPase inhibitory protein using biochemical assay
TLDR
Kinetic analysis showed that Glu30 is involved in the isomerization, whereas Tyr33 contributes to the initial association of IF1 to F1-ATPase and the locking process, where IF1 blocks rotation by inserting its N-terminus.
Su e of the Yeast F1Fo-ATP Synthase Forms Homodimers*
TLDR
Using a histidine-tagged derivative of yeast Su e, Su e-His12, combined with cross-linking and affinity purification approaches, the ability of the yeast Su E protein to form homodimers is directly demonstrated and a model for the molecular basis of the homodimerization of the Su e proteins is proposed.
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