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. 1992 Oct 15;89(20):9386–9390. doi: 10.1073/pnas.89.20.9386

Both purified human 1,N6-ethenoadenine-binding protein and purified human 3-methyladenine-DNA glycosylase act on 1,N6-ethenoadenine and 3-methyladenine.

B Singer 1, A Antoccia 1, A K Basu 1, M K Dosanjh 1, H Fraenkel-Conrat 1, P E Gallagher 1, J T Kuśmierek 1, Z H Qiu 1, B Rydberg 1
PMCID: PMC50136  PMID: 1409645

Abstract

We previously described a protein, isolated from human tissues and cells, that bound to a defined double-stranded oligonucleotide containing a single site-specifically placed 1,N6-ethenoadenine. It was further demonstrated that this protein was a glycosylase and released 1,N6-ethenoadenine. We now find that this enzyme also releases 3-methyladenine from methylated DNA and that 3-methyladenine-DNA glycosylase behaves in the same manner, binding to the ethenoadenine-containing oligonucleotide and cleaving both ethenoadenine and 3-methyladenine from DNA containing these adducts. The rate and extent of glycosylase activities toward the two adducts are similar.

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Selected References

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