ArticleNucleic acids research2015
A structural determinant in the uracil DNA glycosylase superfamily for the removal of uracil from adenine/uracil base pairs.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Structural and Functional Insights into UDGs.Protein and peptide letters · 2025Review
- Structural and functional coupling in cross-linking uracil-DNA glycosylase UDGX.Bioscience reports · 2024Article
- Proteomic Profiles and Protein Network Analysis of Primary Human Leukocytes Revealed Possible Clearance Biomarkers for Staphylococcus aureus Infection.Current microbiology · 2023Article
- 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
- APE2 promotes DNA damage response pathway from a single-strand break.Nucleic acids research · 2018Article
- Identification of a prototypical single-stranded uracil DNA glycosylase from Listeria innocua.DNA repair · 2017Article
- Redox regulation of genome stability by effects on gene expression, epigenetic pathways and DNA damage/repair.Redox biology · 2015Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The uracil DNA glycosylase superfamily consists of several distinct families. Family 2 mismatch-specific uracil DNA glycosylase (MUG) from Escherichia coli is known to exhibit glycosylase activity on three mismatched base pairs, T/U, G/U and C/U. Family 1 uracil N-glycosylase (UNG) from E. coli is an extremely efficient enzyme that can remove uracil from any uracil-containing base pairs including the A/U base pair. Here, we report the identification of an important structural determinant that underlies the functional difference between MUG and UNG. Substitution of a Lys residue at position 68 with Asn in MUG not only accelerates the removal of uracil from mismatched base pairs but also enables the enzyme to gain catalytic activity on A/U base pairs. Binding and kinetic analysis demonstrate that the MUG-K68N substitution results in enhanced ground state binding and transition state interactions. Molecular modeling reveals that MUG-K68N, UNG-N123 and family 5 Thermus thermophiles UDGb-A111N can form bidentate hydrogen bonds with the N3 and O4 moieties of the uracil base. Genetic analysis indicates the gain of function for A/U base pairs allows the MUG-K68N mutant to remove uracil incorporated into the genome during DNA replication. The implications of this study in the origin of life are discussed.
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Registered trials
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