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G:U mismatches resulting from deamination of cytosine are the most common promutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. Recently, a biochemically distinct family of DNA repair enzymes has been identified, which excises both uracil and thymine, but only from mispairs with guanine. Crystal structures of the mismatch-specific uracil DNA-glycosylase (MUG) from E. coli, and of a DNA complex, reveal a remarkable structural and functional homology to UDGs despite low sequence identity. Details of the MUG structure explain its thymine DNA-glycosylase activity and the specificity for G:U/T mispairs, which derives from direct recognition of guanine on the complementary strand.

Type

Journal article

Journal

Cell

Publication Date

09/01/1998

Volume

92

Pages

117 - 129

Keywords

Amino Acid Sequence, Catalysis, Crystallization, Crystallography, X-Ray, DNA, DNA Damage, DNA Glycosylases, DNA Repair, DNA, Complementary, Deoxyribonuclease (Pyrimidine Dimer), Endodeoxyribonucleases, Escherichia coli, Molecular Sequence Data, N-Glycosyl Hydrolases, Nucleic Acid Heteroduplexes, Protein Binding, Sequence Homology, Amino Acid, Substrate Specificity, Uracil-DNA Glycosidase, Viral Proteins