The OGD1 gene, affecting 2-oxoglutarate dehydrogenase in S. cerevisiae, is closely linked to HIS5 on chromosome IX
- 1 January 1990
- journal article
- conference paper
- Published by Springer Nature in Current Genetics
- Vol. 17 (1), 85-88
- https://doi.org/10.1007/bf00313254
Abstract
Ogd1 mutants of Saccharomyces cerevisiae are deficient in mitochondrial 2-oxoglutarate dehydrogenase activity; they cannot grow on glycerol and produce an increased amount of organic acids during growth on glucose as substrate. Using gamma ray-induced rad52-mediated chromosome loss the ogd1 mutation can be assigned to chromosome IX. Tetrad analysis of crosses between ogd1 and other markers on chromosome IX revealed that the OGD1 gene maps on the left arm of this chromosome 1.9 cM from his5.This publication has 18 references indexed in Scilit:
- Structure and regulation of KGD1, the structural gene for yeast alpha-ketoglutarate dehydrogenase.Molecular and Cellular Biology, 1989
- Mapping of the RIB5 gene in Saccharomyces cerevisiae using UV light as an enhancer of rad52-mediated chromosome lossCurrent Genetics, 1988
- Structure of the yeast HIS5 gene responsive to general control of amino acid biosynthesisMolecular Genetics and Genomics, 1987
- Cloning and Characterization of the Gene Encoding Lipoamide Dehydrogenase in Saccharomyces CerevisiaeMicrobiology, 1987
- A mutation affecting lipoamide dehydrogenase, pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase activities in Saccharomyces cerevisiaeMolecular Genetics and Genomics, 1986
- Abnormal amino acid metabolism in mutants of Saccharomyces cerevisiae affected in the initiation of sporulationEuropean Journal of Biochemistry, 1985
- MAPPING CDC MUTATIONS IN THE YEAST S-CEREVISIAE BY RAD52-MEDIATED CHROMOSOME LOSS1985
- Cloning of the HIS5 gene of Saccharomyces cerevisiae by yeast transformationGene, 1981
- Oxidative phosphorylation in a yeast mutant lacking α-ketoglutarate dehydrogenase activityFolia Microbiologica, 1974
- A mutant ofSaccharomyces cerevisiaelacking α-ketoglutarate dehydrogenase activityFEBS Letters, 1972