Journal
BIOCHEMISTRY
Volume 52, Issue 42, Pages 7363-7365Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi401195r
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Funding
- National Science Foundation [MCB-1122098]
- Vanderbilt Training Program in Environmental Toxicology (National Institutes of Health) [T32 ES07028]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1122098] Funding Source: National Science Foundation
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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.
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