ArticleThe Journal of biological chemistry2014
Specificity and catalytic mechanism in family 5 uracil DNA glycosylase.
Article in The Journal of biological chemistry, 2014. 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.
- Crystal structure of MutYX: a novel clusterless adenine DNA glycosylase with a distinct C-terminal domain and 8-oxoguanine recognition sphere.Nucleic acids research · 2025Article
- Structural and functional coupling in cross-linking uracil-DNA glycosylase UDGX.Bioscience reports · 2024Article
- Biochemical and mutational studies of an endonuclease V from the hyperthermophilic crenarchaeon Sulfolobus islandicus REY15A.World journal of microbiology & biotechnology · 2023Article
- DR0022 from Deinococcus radiodurans is an acid uracil-DNA glycosylase.The FEBS journal · 2022Article
- Review
- Repair of Hypoxanthine in DNA Revealed by DNA Glycosylases and Endonucleases From Hyperthermophilic Archaea.Frontiers in microbiology · 2021Review
- Development of a supF-based mutation-detection system in the extreme thermophile Thermus thermophilus HB27.Molecular genetics and genomics : MGG · 2019Article
- Suicide inactivation of the uracil DNA glycosylase UdgX by covalent complex formation.Nature chemical biology · 2019Article
- Identification of a prototypical single-stranded uracil DNA glycosylase from Listeria innocua.DNA repair · 2017Article
- Correlated Mutation in the Evolution of Catalysis in Uracil DNA Glycosylase Superfamily.Scientific reports · 2017Article
- Impact of Rett Syndrome Mutations on MeCP2 MBD Stability.Biochemistry · 2015Article
- A structural determinant in the uracil DNA glycosylase superfamily for the removal of uracil from adenine/uracil base pairs.Nucleic acids research · 2015Article
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Authors and funding
6 authors.
Funding
Abstract
UDGb belongs to family 5 of the uracil DNA glycosylase (UDG) superfamily. Here, we report that family 5 UDGb from Thermus thermophilus HB8 is not only a uracil DNA glycosyase acting on G/U, T/U, C/U, and A/U base pairs, but also a hypoxanthine DNA glycosylase acting on G/I, T/I, and A/I base pairs and a xanthine DNA glycosylase acting on all double-stranded and single-stranded xanthine-containing DNA. Analysis of potentials of mean force indicates that the tendency of hypoxanthine base flipping follows the order of G/I > T/I, A/I > C/I, matching the trend of hypoxanthine DNA glycosylase activity observed in vitro. Genetic analysis indicates that family 5 UDGb can also act as an enzyme to remove uracil incorporated into DNA through the existence of dUTP in the nucleotide pool. Mutational analysis coupled with molecular modeling and molecular dynamics analysis reveals that although hydrogen bonding to O2 of uracil underlies the UDG activity in a dissociative fashion, Tth UDGb relies on multiple catalytic residues to facilitate its excision of hypoxanthine and xanthine. This study underscores the structural and functional diversity in the UDG superfamily.
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