Abstract
Cells exposed to low doses of N-methyl-Nā²-nitro-N-nitroso-guanidine (MNNG) or methyl methanesulphonate (MMS) acquire resistance to both the mutagenic and lethal effects of a challenging dose of the same agents (ref. 1, and ref. 2 for a review). This response, termed adaptation, has been ascribed to the induced synthesis and accumulation of O-6-methyl-guanine (m6G) DNA methyltransferase3,4 which rapidly demethylates the m6G residues induced by the challenging dose3ā5. Mutant studies, however, indicate that mutagenic adaptation and killing adaptation are at least partly under different genetic control and may therefore involve the induction of different repair enzymes6,7. Whereas mutagenic adaptation correlates with the induction of the transferase, the data presented here show that killing adaptation can be ascribed to the induction of a DNA glycosylase. This inducible glycosylase releases the alkylation product 3-methyladenine (m3A) from DNA in vitro as does the constitutive m3A DNA glycosylase previously characterized by Riazuddin and Lindahl8. However, the enzymes are encoded by different genes and appear to have different roles in DNA repair in vivo.
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Evensen, G., Seeberg, E. Adaptation to alkylation resistance involves the induction of a DNA glycosylase. Nature 296, 773ā775 (1982). https://doi.org/10.1038/296773a0
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DOI: https://doi.org/10.1038/296773a0
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