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Nucleic Acids Research, 1981, Vol. 9, No. 13 3089-3103
© 1981

MOLECULAR BIOLOGY

A system in mouse liver for the repair of O6-methylguanine lesions in methylated DNA

James M.Bogden, Alan Eastman and Edward Bresnick

Department of Biochemistry and The Vermont Regional Cancer Center, University of Vermont College of Medicine Burlington, VT 05405, USA

Received May 25, 1981. An activity from mouse liver which catalyzes the disappearance of 06- methylguanine from DNA methylated with methylnitrosourea has been partially purified by ammonium sulfate fractionation and DNA-cellulose chromatography. The activity does not require divalent metal ions and is not affected by EDTA. It is specific for the repair of O6-methylguanine lesions and does not affect the removal of 7-methylguanine, 7-methyladenine or 3-methyladenine. The disappearance of 06-methylguanine is linear with respect to the concentration of protein and is dependent on incubation temperature. The kinetics and substrate dependence experiments suggest that the protein factor is product-inactivated. Amino acid analysis of hydrolysates of protein obtained after incubation of methylated DNA with the protein factor indicates the presence of radiolabeled S-methyl-L-cysteine, suggesting that during the repair of O6-methylguanine from methylated DNA, the methyl group is transferred to a sulfhydryl of a cysteine residue of a protein. This represents the first such demonstration in a mammalian system.


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