Mechanisms of Base Selection by Human Single-strand Selective Monofunctional Uracil-DNA Glycosylase*
نویسندگان
چکیده
From Department of Basic Sciences, Loma Linda University School of Medicine, Loma Linda, CA, and Department of Chemistry, California Institute of Technology, Pasadena, CA Running head: hSMUG1 substrate selectivity *This project was supported in part by funds from the National Institutes of Health Address correspondence to: Lawrence Sowers, PhD, 11021 Campus Street, Rm 101, Loma Linda, CA 92350. Fax: 909-558-4035; E-mail: [email protected]
منابع مشابه
Mechanisms of base selection by human single-stranded selective monofunctional uracil-DNA glycosylase.
hSMUG1 (human single-stranded selective monofunctional uracil-DNA glyscosylase) is one of three glycosylases encoded within a small region of human chromosome 12. Those three glycosylases, UNG (uracil-DNA glycosylase), TDG (thymine-DNA glyscosylase), and hSMUG1, have in common the capacity to remove uracil from DNA. However, these glycosylases also repair other lesions and have distinct substra...
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Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1), previously thought to be a backup enzyme for uracil-DNA glycosylase, has recently been shown to excise 5-hydroxyuracil (hoU), 5-hydroxymethyluracil (hmU) and 5-formyluracil (fU) bearing an oxidized group at ring C5 as well as an uracil. In the present study, we used site-directed mutagenesis to construct a series of mutants ...
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PURPOSE The aim of this study was to determine the excision efficiency of hSMUG1 (human single-strand-selective monofunctional uracil-DNA glycosylase) for 5-formyluracil (fU), a major thymine lesion formed by ionizing radiation, opposite all normal bases in DNA, to possibly explain mutation induction by fU in the DNA of mammalian cells. MATERIALS AND METHODS An enzymatically [(32)P]labelled f...
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A wide range of cytotoxic and mutagenic DNA bases are removed by different DNA glycosylases, which initiate the base excision repair pathway. DNA glycosylases cleave the N-glycosylic bond between the target base and deoxyribose, thus releasing a free base and leaving an apurinic/apyrimidinic (AP) site. In addition, several DNA glycosylases are bifunctional, since they also display a lyase activ...
متن کاملBiochemical and structural characterization of the glycosylase domain of MBD4 bound to thymine and 5-hydroxymethyuracil-containing DNA
Active DNA demethylation in mammals occurs via hydroxylation of 5-methylcytosine to 5-hydroxymethylcytosine (5hmC) by the ten-eleven translocation family of proteins (TETs). 5hmC residues in DNA can be further oxidized by TETs to 5-carboxylcytosines and/or deaminated by the Activation Induced Deaminase/Apolipoprotein B mRNA-editing enzyme complex family proteins to 5-hydromethyluracil (5hmU). E...
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تاریخ انتشار 2009