Action mechanism of human SMUG1 uracil-DNA glycosylase.
The DNA lesions resulting from deamination or oxidation of bases are generally repaired by the base excision repair pathway initiated by damage-specific DNA glycosylases. Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) present in vertebrates and insects excises not only uracil but also uracil derivatives bearing an oxidized group at ring-C5 from DNA, indicating roles in the repair of both deamination and oxidation damage to DNA. In the present study, we have constructed a series of active site mutants of human SMUG1 and analyzed the catalytic and precision damage recognition mechanisms.
Matsubara
Mayumi
M
Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan.
Tanaka
Tamon
T
Terato
Hiroaki
H
Ide
Hiroshi
H
D001665:Binding Sites; D002384:Catalysis; D004260:DNA Repair; D006801:Humans; D009154:Mutation; D051981:Uracil-DNA Glycosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
C498095:SMUG1 protein, human; D051981:Uracil-DNA Glycosidase