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M010641200v1
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Papers In Press, published online ahead of print January 22, 2001
J. Biol. Chem, 10.1074/jbc.M010641200
Submitted on November 26, 2000
Revised on January 4, 2001
Accepted on January 19, 2001

Base excision and DNA binding activities of human alkyladenine DNA glycosylase are sensitive to the base paired with a lesion

Clint W. Abner, Albert Y. Lau, Tom Ellenberger, and Linda B. Bloom

Biochemistry & Molecular Biology, University of Florida, Gainesville, FL 32610-0245

Corresponding Author: lbloom{at}ufl.edu

The human alkyladenine DNA glycosylase (hAAG) has a broad substrate specificity, excising a structurally diverse group of damaged purines from DNA. To more clearly define the structural and mechanistic bases for substrate specificity of hAAG, kinetics of excision and DNA binding activities were measured for several different damaged and undamaged purines within identical DNA sequence contexts. We found that 1,N6-ethenoadenine (epsilon A) and hypoxanthine (Hx) were excised relatively efficiently while 7,8-dihydro-8-oxo-2?-deoxyguanine, O6-methylguanine, adenine, and guanine were not. Single-turnover kinetics of excision of Hx and epsilon A paired with T showed that excision of Hx was about 4 times faster than epsilon A while binding assays showed that the binding affinity was about 5 times greater for epsilon A than for Hx. The opposing pyrimidine base had a significant effect on the kinetics of excision and DNA binding affinity of Hx but a small effect on those for epsilon A. Surprisingly, replacing a T with U opposite Hx dramatically reduced the excision rate by a factor of 15 and increased the affinity by a factor of 7 to 8. The binding affinity of hAAG to a DNA product containing an abasic site was similar to that for an Hx lesion.


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