ArticleNucleic acids research2015
Thymine DNA glycosylase exhibits negligible affinity for nucleobases that it removes from DNA.
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 21 papers.
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Who cites it
21 citing papers in PubMed, 35 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
- α-ketoglutarate/succinate ratio imbalance impairs thymine DNA glycosylase function and base excision repair process increasing susceptibility to pancreatic cancer.Cell death & disease · 2026Article
- Observing nucleotide flipping in DNA using indirect 2'-F nucleotide probes and 19F NMR.Nucleic acids research · 2025Article
- Targeting the chromatin structural changes of antitumor immunity.Journal of pharmaceutical analysis · 2024Review
- Structural snapshots of base excision by the cancer-associated variant MutY N146S reveal a retaining mechanism.Nucleic acids research · 2023Article
- Characterizing inhibitors of human AP endonuclease 1.PloS one · 2023Article
- Computational investigations on target-site searching and recognition mechanisms by thymine DNA glycosylase during DNA repair process.Acta biochimica et biophysica Sinica · 2022Review
- Structural Insights into the Mechanism of Base Excision by MBD4.Journal of molecular biology · 2021Article
- The role of RNA mInternational journal of biological sciences · 2021Review
- Excision of 5-Carboxylcytosine by Thymine DNA Glycosylase.Journal of the American Chemical Society · 2019Article
- Defining the Role of Nucleotide Flipping in Enzyme Specificity UsingJournal of the American Chemical Society · 2019Article
- Base-flipping dynamics from an intrahelical to an extrahelical state exerted by thymine DNA glycosylase during DNA repair process.Nucleic acids research · 2018Article
- Defining the impact of sumoylation on substrate binding and catalysis by thymine DNA glycosylase.Nucleic acids research · 2018Article
- Dynamics of the excised base release in thymine DNA glycosylase during DNA repair process.Nucleic acids research · 2018Article
- TET-mediated active DNA demethylation: mechanism, function and beyond.Nature reviews. Genetics · 2017Review
- Article
- Kinetic Methods for Studying DNA Glycosylases Functioning in Base Excision Repair.Methods in enzymology · 2017Article
- Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues.Nucleic acids research · 2016Article
- Article
- Role of Base Excision "Repair" Enzymes in Erasing Epigenetic Marks from DNA.Chemical reviews · 2016Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Thymine DNA Glycosylase (TDG) performs essential functions in maintaining genetic integrity and epigenetic regulation. Initiating base excision repair, TDG removes thymine from mutagenic G ·: T mispairs caused by 5-methylcytosine (mC) deamination and other lesions including uracil (U) and 5-hydroxymethyluracil (hmU). In DNA demethylation, TDG excises 5-formylcytosine (fC) and 5-carboxylcytosine (caC), which are generated from mC by Tet (ten-eleven translocation) enzymes. Using improved crystallization conditions, we solved high-resolution (up to 1.45 Å) structures of TDG enzyme-product complexes generated from substrates including G·U, G·T, G·hmU, G·fC and G·caC. The structures reveal many new features, including key water-mediated enzyme-substrate interactions. Together with nuclear magnetic resonance experiments, the structures demonstrate that TDG releases the excised base from its tight product complex with abasic DNA, contrary to previous reports. Moreover, DNA-free TDG exhibits no significant binding to free nucleobases (U, T, hmU), indicating a Kd >> 10 mM. The structures reveal a solvent-filled channel to the active site, which might facilitate dissociation of the excised base and enable caC excision, which involves solvent-mediated acid catalysis. Dissociation of the excised base allows TDG to bind the beta rather than the alpha anomer of the abasic sugar, which might stabilize the enzyme-product complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.