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Disruption of the gene encoding subunit VI of yeast cytochrome bc 1 complex causes respiratory deficiency of cells with reduced cytochrome c levels
Author(s) -
Kim Chong H.,
Zitomer Richard S.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81511-l
Subject(s) - complementation , mutant , yeast , protein subunit , biology , saccharomyces cerevisiae , gene , mitochondrion , biochemistry , hspa2 , respiratory chain , wild type , cytochrome , microbiology and biotechnology , enzyme , peptide sequence
A double mutant of Saccharomyces cerevisiae , in which CYCl gene is deleted and the chromosomal copy of the 17 kDa protein gene is disrupted, has been constructed. This mutant cannot grow on nonfermentable carbon sources, but normal growth can be restored by complementation of either mutation with a yeast vector containing either the wild‐type 17 kDa protein gene or the CYCl gene. These results show that although the 17 kDa protein, subunit VI of yeast cytochrome bc 1 complex is dispensable for yeast mitochondrial respiration in cells with the wild‐type levels of cytochrome c , the 17 kDa protein is essential for respiration when the level of cytochrome c is limited, indicating that is plays a role in electron transport. This glycerol − phenotype of the double mutant can serve as the basis for further genetic studies on the function of the 17 kDa protein in yeast mitochondria and may provide insight into the physiological function of the hinge protein, the counterpart of the yeast 17 kDa protein, in beef heart mitochondria.