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Nucleic Acids Research, 1987, Vol. 15, No. 24 10355-10371
© 1987

Articles

Molecular characterization of the Saccharomyces cerevisiae dihydrofolate reductase gene (DFRl)

Peter A. Lagosky1,*, Gareth R. Taylor2 and Robert H. Haynes$

Department of Biology, York University Toronto, Ontario M3J 1P3, Canada

*To whom correspondence should be addressed

Received August 25, 1987. Revised November 18, 1987. Accepted November 18, 1987.

The complete nucleotide sequence of a 1957 bp DNA fragment containing the dihydrofolate reductase gene (DFRl) of the yeast Saccharomyces cerevisiae is presented. Within this region a single open reading frame of 633 base pairs was found which is capable of encoding a 211 amino acid residue protein with a calculated Mr of 24,233. The amino acid sequence derived from the yeast DFRl gene shows limited homology with sequences from both eukaryotic and non-eukaryotic DHFR enzymes. Northern blot hybridization reveals that the mRNA from this gene is a 900 base polyadenylated transcript. Yeast strains containing the cloned DFRl gene on multicopy number shuttle vector plasmids show dramatically enhanced methotrexate resistance. Consensus DNA sequences responsible for RNA polymerase II interaction and general amino acid control in S. cerevisiae are located within the 5'-noncoding region with respect to the open reading frame. The DNA fragment containing these sequences has been shown to be necessary for DFRl gene expression in both S. cerevisiae and E. coli.

1Present address: Cangene Corporation, Mississauga, Ontario L4V 1T4

2Present address: Mt Sinai Research Institute, Division of Molecular and Developmental Biology, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada

$To whom reprint requests should be addressed


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