Uracil-DNA Glycosylases in DNA Repair Mechanisms
Summary
Uracil-DNA glycosylases (UDGs) are a family of specialised enzymes that safeguard genomic integrity by recognising and excising uracil residues misincorporated into DNA or arising from cytosine deamination. Acting as the initiating step in the base-excision repair pathway, UDGs cleave the N-glycosidic bond to generate an abasic site, which is then processed by downstream enzymes to restore the correct nucleotide sequence. Across all domains of life, multiple UDG families share a common structural fold yet display diverse active-site architectures that determine substrate specificity and reaction kinetics. Rapid removal of uracil from DNA prevents mutagenic G:U mismatches, maintains faithful transmission of genetic information and underpins cellular responses to environmental stress. Beyond their fundamental role in DNA maintenance, UDGs participate in antiviral immunity, influence the efficacy of chemotherapeutic agents that induce uracil-related lesions and serve as potential targets for inhibitor design in cancer and infectious-disease contexts.
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Uracil-DNA Glycosylases in DNA Repair Mechanisms publication trend
The graph below shows the total number of articles in uracil-dna glycosylases in dna repair mechanisms across all publications each year (not limited to Nature Index journals).
Technical terms
Base-excision repair: DNA repair pathway initiated by removal of damaged or inappropriate bases, leaving an abasic site that is further processed to restore the correct nucleotide.
Uracil: A pyrimidine base normally found in RNA; appears in DNA through cytosine deamination or misincorporation of dUTP, leading to mutagenic lesions.
Apurinic/apyrimidinic site: An abasic position in DNA created when a glycosylase cleaves the glycosidic bond of a damaged base, requiring downstream repair enzymes.
dUTPase: Enzyme that hydrolyses dUTP to dUMP and pyrophosphate, preventing uracil misincorporation into DNA during replication.
References
- Mutational and structural analyses of UdgX: insights into the active site pocket architecture and its evolution. Nucleic Acids Research (2023).
- DUF99 family proteins are novel endonucleases that cleave deoxyuridine on DNA substrates. Journal of Biological Chemistry (2024).
- A Multimodal Approach towards Genomic Identification of Protein Inhibitors of Uracil-DNA Glycosylase. Viruses (2023).
- The α/β fold uracil DNA glycosylases: a common origin with diverse fates. Genome Biology (2000).
- Uracil within DNA: an actor of antiviral immunity. Retrovirology (2008).
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