Involvement of 3-methyladenine DNA glycosylases Mag1p and Mag2p in base excision repair of methyl methanesulfonate-damaged DNA in the fission yeast Schizosaccharomyces pombe

• Published in: Genes & Genetic Systems Vol. 82; no. 6; pp. 489 - 494
• Main Authors: Kanamitsu, K.(Okayama Univ. of Science (Japan)), Tanihigashi, H, Tanita, Y, Inatani, S, Ikeda, S
• Format: Journal Article
• Language: English
• Published: Japan The Genetics Society of Japan 2007; Japan Science and Technology Agency
• Subjects: 3-methyladenine DNA glycosylase; Alkylation; alkylation damage; Base excision repair; DNA damage; DNA Damage - physiology; DNA glycosylase; DNA Glycosylases - genetics; DNA Glycosylases - metabolism; DNA Repair; Enzymes; Escherichia coli; EXPRESION GENICA; EXPRESSION DES GENES; Gene deletion; GENE EXPRESSION; Genetic analysis; Homology; mag1; mag2; Methyl methanesulfonate; Methyl Methanesulfonate - toxicity; MMS; Mutagens - toxicity; MUTANT; MUTANTES; MUTANTS; NTH1 protein; Nucleotide excision repair; REPAIRING; REPARACION; REPARATION; Schizosaccharomyces - drug effects; Schizosaccharomyces - enzymology; Schizosaccharomyces - genetics; SCHIZOSACCHAROMYCES POMBE; Schizosaccharomyces pombe Proteins - genetics; Schizosaccharomyces pombe Proteins - metabolism

Schizosaccharomyces pombe has two paralogues of 3-methyladenine DNA glycosylase, Mag1p and Mag2p, which share homology with Escherichia coli AlkA. To clarify the function of these redundant enzymes in base excision repair (BER) of alkylation damage, we performed several genetic analyses. The mag1 an...