Isolation of the catalase A gene of Saccharomyces cerevisiae by complementation of the cta1 mutation - PubMed (original) (raw)
- PMID: 3897793
- DOI: 10.1007/BF00383315
Isolation of the catalase A gene of Saccharomyces cerevisiae by complementation of the cta1 mutation
G Cohen et al. Mol Gen Genet. 1985.
Abstract
As a first step in an analysis of the DNA regions involved in the control of the catalase A gene of Saccharomyces cerevisiae by glucose, heme, and oxygen this gene has been cloned. Catalase A-deficient mutants were obtained by UV mutagenesis of a ctt1 mutant strain specifically lacking catalase T. All the catalase A-deficient mutants obtained fall into one complementation group. The single recessive mutation causing specific lack of catalase A was designated cta1. Several overlapping DNA fragments complementing the cta1 mutation were obtained by transforming ctt1 cta1 double mutants with a yeast gene library in vector YEp13. Hybrid selection of RNA with the help of one of the cloned DNAs followed by in vitro translation of this RNA and identification of the protein synthesized with catalase A-specific antibodies showed that the catalase A structural gene has been cloned. A single copy of this gene is present in the yeast genome. Transcription of the catalase A gene cloned into vector YEp13 is repressed by glucose. The DNA isolated hybridizes to a 1.6 kb polyA+-RNA virtually absent from heme-deficient cells, presumably catalase A mRNA.
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References
- Proc Natl Acad Sci U S A. 1980 Apr;77(4):2119-23 - PubMed
- Acta Microbiol Pol. 1980;29(3):199-212 - PubMed
- Nucleic Acids Res. 1981 Jul 10;9(13):2989-98 - PubMed
- Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201-5 - PubMed
- Curr Genet. 1984 Jan;8(1):45-8 - PubMed
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