Analysis of COX2 mutants reveals cytochrome oxidase subassemblies in yeast
| Autor: | Brigitte Meunier, Ingrid Bourges, Susannah Horan, Jan-Willem Taanman |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
chemistry.chemical_classification
biology Protein subunit Saccharomyces cerevisiae Mutant Electron Transport Complex IV Cell Biology Mitochondrion biology.organism_classification Biochemistry Yeast Protein Subunits Enzyme chemistry Mutation biology.protein Cytochrome c oxidase Molecular Biology Research Article |
| Popis: | Cytochrome oxidase catalyses the reduction of oxygen to water. The mitochondrial enzyme contains up to 13 subunits, 11 in yeast, of which three, Cox1p, Cox2p and Cox3p, are mitochondrially encoded. The assembly pathway of this complex is still poorly understood. Its study in yeast has been so far impeded by the rapid turnover of unassembled subunits of the enzyme. In the present study, immunoblot analysis of blue native gels of yeast wild-type and Cox2p mutants revealed five cytochrome oxidase complexes or subcomplexes: a, b, c, d and f; a is likely to be the fully assembled enzyme; b lacks Cox6ap; d contains Cox7p and/or Cox7ap; f represents unassembled Cox1p; and c, observed only in the Cox2p mutants, contains Cox1p, Cox3p, Cox5p and Cox6p and lacks the other subunits. The identification of these novel cytochrome oxidase subcomplexes should encourage the reexamination of other yeast mutants. |
| Databáze: | OpenAIRE |
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