| Autor: |
Schoppink PJ; Laboratory of Biochemistry, University of Amsterdam, The Netherlands., Hemrika W, Reynen JM, Grivell LA, Berden JA |
| Jazyk: |
angličtina |
| Zdroj: |
European journal of biochemistry [Eur J Biochem] 1988 Apr 05; Vol. 173 (1), pp. 115-22. |
| DOI: |
10.1111/j.1432-1033.1988.tb13974.x |
| Abstrakt: |
The single nuclear gene encoding the 17-kDa subunit VI of yeast ubiquinol: cytochrome c oxidoreductase has been inactivated by one-step gene disruption. Disruption was verified by Southern blot analysis of nuclear DNA and immunoblotting. Cells lacking the 17-kDa protein are still capable of growth on glycerol and they contain all other subunits of complex III at wild-type levels, implying that the 17-kDa subunit is not essential for either assembly of complex III, or its function. In vitro, electron transport activity of complex III of mutant cells is about 40% of the wild-type complex, but for the total respiratory chain no significant differences in activity was measured between mutant and wild type. The energy-transducing capacity of the complex is not reduced in the absence of the 17-kDa protein. In a relatively high proportion of the transformants, disruption of the 17-kDa gene was accompanied by the appearance of a second mutation causing a petite phenotype. In these cells which lack cytochrome b, the presence of the 17-kDa protein (after complementation) results in stabilization of cytochrome c1. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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