Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase.
Using degenerate oligodeoxyribonucleotides based on the N-terminal amino acid (aa) sequence of a yeast glutathione reductase (GR) CNBr-generated peptide fragment and a conserved C-terminal region of known GR aa sequences, the yeast gene encoding GR, GLR1, was isolated using PCR followed by screening of a yeast genomic DNA plasmid library. GLR1 encodes a 467-aa protein with a deduced M(r) of 51,545. Comparison with Escherichia coli and human GR sequences reveals 49.8% aa identity. Yeast cells transformed with a multicopy plasmid containing the genomic clone overproduced GR activity sixfold. GLR1 was found not to be an essential gene.
Collinson
L P
LP
School of Biochemistry and Molecular Genetics, University of New South Wales, Sydney, Australia.
Dawes
I W
IW
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D015966:Gene Expression Regulation, Fungal; D005800:Genes, Fungal / Q000235:genetics*; D005980:Glutathione Reductase / Q000096:biosynthesis / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics*; D017422:Sequence Analysis, DNA; D017384:Sequence Deletion / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013172:Spores, Fungal / Q000254:growth & development
D005980:Glutathione Reductase