Abstract
We have begun to develop the fission yeast, Schizosaccharomyces pombe, as a eukaryotic model for cellular defenses against alkylating agents. Here we describe the cloning and characterization of a cDNA, designated mag1, encoding a S. pombe 3-methyladenine (3MeA) DNA glycosylase. 3MeA DNA glycosylases in Escherichia coli are encoded by alkA and tag. S. pombe mag1 was cloned by its ability to reverse the alkylation-sensitive phenotype of an alkA tag E. coli double mutant. The expression of S. pombe magl in E. coli confers partial resistance to alkylating agents that produce methyl, ethyl and propyl lesions, and Magl production produces 3MeA DNA glycosylase activity. In contrast to the E. coli alkA and Saccharomyces cerevisiae MAG genes, expression of S. pombe magl was not appreciably induced by alkylating agents. The magl cDNA encodes a protein of 228 amino acids (aa) that shares similarity with 3MeA DNA glycosylases from E. coli (AlkA), Bacillus subtilis (BsAlkA) and S. cerevisiae (MAG). A consensus sequence of 9 aa common to these microbial 3MeA DNA glycosylases is discussed.
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