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National Institute of Environmental Health Sciences

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Publication Detail

Title: Depurination of N7-methylguanine by DNA glycosylase AlkD is dependent on the DNA backbone.

Authors: Rubinson, Emily H; Christov, Plamen P; Eichman, Brandt F

Published In Biochemistry, (2013 Oct 22)

Abstract: DNA glycosylase AlkD excises N7-methylguanine (7mG) by a unique but unknown mechanism, in which the damaged nucleotide is positioned away from the protein and the phosphate backbone is distorted. Here, we show by methylphosphonate substitution that a phosphate proximal to the lesion has a significant effect on the rate enhancement of 7mG depurination by the enzyme. Thus, instead of a conventional mechanism whereby protein side chains participate in N-glycosidic bond cleavage, AlkD remodels the DNA into an active site composed exclusively of DNA functional groups that provide the necessary chemistry to catalyze depurination.

PubMed ID: 24090276 Exiting the NIEHS site

MeSH Terms: Catalysis; Catalytic Domain; Crystallography, X-Ray; DNA Glycosylases/chemistry; DNA Glycosylases/metabolism*; DNA Repair*; DNA/chemistry*; DNA/metabolism; Guanine/analogs & derivatives*; Guanine/chemistry; Guanine/metabolism; Humans; Models, Molecular; Protein Conformation; Purines/metabolism*

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