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- Title
The a-subunit of the mitochondrial F<sub>1</sub> ATPase interacts directly with the assembly factor Atp12p.
- Authors
Zhen-Guo Wang; Sheluho, Dmitry; Gatti, Domenico L.; Ackerman, Sharon H.
- Abstract
The Atp12p protein of Saccharomyces cerevisiae is required for the assembly of the F1 component of the mitochondrial F1F0 ATP synthase. In this report, we show that the F1 α-subunit co-precipitates and co-purifies with a tagged form of Atp12p adsorbed to affinity resins. Moreover; sedimentation analysis indicates that in the presence of the F1 α-subunit, Atp12p behaves as a particle of higher mass than is observed in the absence of the α-subunit. Yeast two-hybrid screens confirm the direct association of Atp12p with the α-subunit and indicate that the binding site for the assembly factor lies in the nucleotide-binding domain of the A-subunit, between Asp133 and Leu322. These studies provide the basis for a model of F1 assembly in which Atp12p is released from the α-subunit in exchange for a β-subunit to form the interface that contains the non-catalytic adenine nucleotide-binding site.
- Subjects
PROTEINS; SACCHAROMYCES cerevisiae; MITOCHONDRIA; ADENOSINE triphosphate; SEDIMENTATION analysis; BINDING sites; ADENINE nucleotides
- Publication
EMBO Journal, 2000, Vol 19, Issue 7, p1486
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/19.7.1486