Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases

Rabindra Roy, S. J. Kennel, Sankar Mitra

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair protein, removes several N-alkylpurine adducts, hypoxanthine, cyclic ethenoadducts of adenine, guanine and cytosine and 8-oxoguanine from DNA. The recombinant human and mouse MPGs, purified from Escherichia coli, show a significant difference in substrate preference. While both proteins prefer 3-methyladenine over other N-alkylpurines in DNA, the mouse MPG removes 7-methylguanine and 3-methylguanine at an ~2- to 3-fold higher rate than the human protein when adjusted for equal activity for the release of 3-methyladenine from DNA. Hybrid recombinant proteins containing N-terminal and C-terminal halves of the human and mouse glycosylases were partially purified from MPG-negative E.coli. Their substrate preferences suggest that the N-terminal half is more critical for the recognition of 3-methylguanine and 7-methylguanine.

Original languageEnglish (US)
Pages (from-to)2177-2182
Number of pages6
JournalCarcinogenesis
Volume17
Issue number10
DOIs
StatePublished - Oct 1996

ASJC Scopus subject areas

  • Cancer Research

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