Biogenesis of mitochondria. Oli2 mutations affecting the coupling of oxidation to phosphorylation in Saccharomyces cerevisiae
| Autor: | Henry R. Roberts, Wan Mee Choo, Mark Murphy, H.Bruce Lukins, Sangkot Marzuki, Ian Macreadie, Anthony W. Linnane |
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| Rok vydání: | 1980 |
| Předmět: |
Carbonyl Cyanide m-Chlorophenyl Hydrazone
Chemical Phenomena Cytochrome ATPase Saccharomyces cerevisiae Mutant Biophysics Oxidative phosphorylation Mitochondrion Biochemistry Oxidative Phosphorylation Electron Transport Complex IV Oxygen Consumption Cytochrome c oxidase DNA Fungal Adenosine Triphosphatases biology ATPase complex Cell Biology biology.organism_classification Molecular biology Mitochondria Chemistry Mutation biology.protein |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. 592:431-444 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/0005-2728(80)90090-0 |
| Popis: | 1. 1. Two oligomycin-resistant strains of Saccharomyces cerevisiae have been isolated and shown to have mutations in the oli2 region of the mitochondrial DNA. On solid media containing a non-fermentable energy source, the mutant strains were able to grow only slowly at 28°C and not at all at 18°C or 36°C. 2. 2. When grown in a glucose-limited chemostat at 28°C, the mutant strains were almost completely defective in oxidative metabolism. The mutant mitochondria contained significant levels of all respiratory enzymes, and an active, oligomycin-sensitive ATPase, but the ATP- 32 P i exchange activity and P : O ratio were very low. 3. 3. The mutations in these strains are genetically closely linked to mit − mutations which have been shown to affect a 20 000-dalton ATPase subunit (Roberts, H., Choo, W.M., Murphy, M., Marzuki, S., Lukins, H.B. and Linnane, A.W. (1979) FEBS Lett. 108, 501–504). Since the mitochondrial ATPase in these mutant strains appears to be fully assembled, the defect in the coupling mechanism is probably a result of a small alteration in the structure of the 20 000-dalton ATPase subunit. 4. 4. When the mutant strains were grown at 18°C, the mitochondria had very low cytochrome oxidase activities, and reduced levels of cytochrome aa 3 . The largest subunit ( M r 40 000) of this enzyme was not synthesized. |
| Databáze: | OpenAIRE |
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