ArticleThe Journal of biological chemistry2010
Identification of Escherichia coli mismatch-specific uracil DNA glycosylase as a robust xanthine DNA glycosylase.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Robust excision of different purine lesions by homologs thymine DNA glycosylase and mismatch-specific uracil DNA-glycosylase.The Journal of biological chemistry · 2026Article
- Structural and functional coupling in cross-linking uracil-DNA glycosylase UDGX.Bioscience reports · 2024Article
- DR0022 from Deinococcus radiodurans is an acid uracil-DNA glycosylase.The FEBS journal · 2022Article
- Role of endonuclease III enzymes in uracil repair.Mutation research · 2019Article
- Identification of a prototypical single-stranded uracil DNA glycosylase from Listeria innocua.DNA repair · 2017Article
- Article
- A structural determinant in the uracil DNA glycosylase superfamily for the removal of uracil from adenine/uracil base pairs.Nucleic acids research · 2015Article
- Mechanisms for enzymatic cleavage of the N-glycosidic bond in DNA.Organic & biomolecular chemistry · 2014Review
- Specificity and catalytic mechanism in family 5 uracil DNA glycosylase.The Journal of biological chemistry · 2014Article
- Endonuclease V: an unusual enzyme for repair of DNA deamination.Cellular and molecular life sciences : CMLS · 2013Review
- Defects in purine nucleotide metabolism lead to substantial incorporation of xanthine and hypoxanthine into DNA and RNA.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- New family of deamination repair enzymes in uracil-DNA glycosylase superfamily.The Journal of biological chemistry · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The gene for the mismatch-specific uracil DNA glycosylase (MUG) was identified in the Escherichia coli genome as a sequence homolog of the human thymine DNA glycosylase with activity against mismatched uracil base pairs. Examination of cell extracts led us to detect a previously unknown xanthine DNA glycosylase (XDG) activity in E. coli. DNA glycosylase assays with purified enzymes indicated the novel XDG activity is attributable to MUG. Here, we report a biochemical characterization of xanthine DNA glycosylase activity in MUG. The wild type MUG possesses more robust activity against xanthine than uracil and is active against all xanthine-containing DNA (C/X, T/X, G/X, A/X and single-stranded X). Analysis of potentials of mean force indicates that the double-stranded xanthine base pairs have a relatively narrow energetic difference in base flipping, whereas the tendency for uracil base flipping follows the order of C/U > G/U > T/U > A/U. Site-directed mutagenesis performed on conserved motifs revealed that Asn-140 and Ser-23 are important determinants for XDG activity in E. coli MUG. Molecular modeling and molecular dynamics simulations reveal distinct hydrogen-bonding patterns in the active site of E. coli MUG that account for the specificity differences between E. coli MUG and human thymine DNA glycosylase as well as that between the wild type MUG and the Asn-140 and Ser-23 mutants. This study underscores the role of the favorable binding interactions in modulating the specificity of DNA glycosylases.
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