title: Action mechanism of human SMUG1 uracil-DNA glycosylase.
abstract: 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.
authors.affiliation: Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan.
authors.forename: Mayumi
authors.initials: M
authors.lastname: Matsubara
authors.forename: Tamon
authors.initials: T
authors.lastname: Tanaka
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Terato
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Ide
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D004260:DNA Repair; D006801:Humans; D009154:Mutation; D051981:Uracil-DNA Glycosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: C498095:SMUG1 protein, human; D051981:Uracil-DNA Glycosidase