Journal Article

Distinct substrate preference of human and mouse <i>N</i>-methylpurine-DNA glycosylases

Rabindra Roy, S. J. Kennel and Sankar Mitra

in Carcinogenesis

Volume 17, issue 10, pages 2177-2182
Published in print October 1996 | ISSN: 0143-3334
Published online October 1996 | e-ISSN: 1460-2180 | DOI: http://dx.doi.org/10.1093/carcin/17.10.2177
Distinct substrate preference of human and mouse
                    N-methylpurine-DNA glycosylases

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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 Esch-erichia 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.

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Subjects: Clinical Cytogenetics and Molecular Genetics

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