Synthesis of the Proteins of Complex III of the Mitochondrial Respiratory Chain in Heme-Deficient Cells
| Autor: | Ching-I. P. Lin, Edith G. Gollub, Diana S. Beattie |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Antiserum
Gel electrophoresis Protein subunit Respiratory chain Heme Saccharomyces cerevisiae Biology Biochemistry Molecular biology Mitochondria Molecular Weight Electron Transport Complex III Kinetics chemistry.chemical_compound Mitochondrial respiratory chain chemistry Cytochrome C1 Multienzyme Complexes Coenzyme Q – cytochrome c reductase NADH NADPH Oxidoreductases Quinone Reductases |
| Zdroj: | European Journal of Biochemistry. 128:309-313 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1982.tb06966.x |
| Popis: | The presence of several proteins of complex III of the respiratory chain has been demonstrated in mitochondria from a mutant of Saccharomyces cerevisiae lacking 5-aminolevulinic acid synthase and, hence, devoid of heme. The two 'core' proteins, apocytochrome b and the iron-sulfur protein, were observed in equal amounts in the heme-deficient and heme-sufficient cells with antiserum against complex III and the sensitive immuno-transfer technique. In addition, three other bands were detected with the complex III antiserum in the mitochondria from the cells lacking heme. One of these has a molecular weight similar to that reported for a precursor form of cytochrome c1. By contrast, when mitochondria from the heme-deficient cells were solubilized with mild detergents and treated with the complex III antiserum, almost no immunoprecipitation was obtained above that obtained with control serum. The presence of only one major labeled band with a molecular weight similar to subunit I was observed after gel electrophoresis. These results suggest that heme may be necessary for proper processing of the apoprotein of cytochrome c1 and for the assembly into the membrane of the subunits of complex III, rather than for the synthesis of the proteins. |
| Databáze: | OpenAIRE |
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