Article
Characterization of domain interfaces in monomeric and dimeric ATP synthase.
Molecular & cellular proteomics : MCP - 1 May 2008
Wittig Ilka, Velours Jean, Stuart Rosemary, Schägger Hermann
Abstract excerpt
We disassembled monomeric and dimeric yeast ATP synthase under mild conditions to identify labile proteins and transiently stable subcomplexes that had not been observed before. Specific removal of subunits alpha, beta, oligomycin sensitivity conferring protein (OSCP), and h disrupted the ATP synthase at the gamma-alpha(3)beta(3) rotor-stator interface. Loss of two F(1)-parts from dimeric ATP synthase led to the...
Topics
- Adaptor Proteins, Signal Transducing
- Adenosine Triphosphatases
- Carrier Proteins
- Dimerization
- Membrane Proteins
- Mitochondrial Proteins
- Mitochondrial Proton-Translocating ATPases
- Multienzyme Complexes
- Mutation
- Protein Structure, Tertiary
- Protein Subunits
- Proteins
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- ATPase Inhibitory Protein