ArticleJournal of the American Chemical Society2018
Exploiting Substrate Promiscuity To Develop Activity-Based Probes for Ten-Eleven Translocation Family Enzymes.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- DREAMS illuminates spatial DNA and RNA modification landscapes.Nature cell biology · 2026Article
- Unnatural Cytosine Analogs Potentiate a Customizable, Enzymatic Method for Integrated Epigenetic and Four-Base Genetic Sequencing.Journal of the American Chemical Society · 2026Article
- Histone probes for reader and eraser investigations.Chemical science · 2025Review
- A general approach for activity-based protein profiling of oxidoreductases with redox-differentiated diarylhalonium warheads.Chemical science · 2025Article
- Chemoproteomic Approaches to Studying RNA Modification-Associated Proteins.Accounts of chemical research · 2023Article
- Chemical Approaches To Investigate Post-transcriptional RNA Regulation.ACS chemical biology · 2023Review
- Direct enzymatic sequencing of 5-methylcytosine at single-base resolution.Nature chemical biology · 2023Article
- Reactivity-dependent profiling of RNA 5-methylcytidine dioxygenases.Nature communications · 2022Article
- How Human TET2 Enzyme Catalyzes the Oxidation of Unnatural Cytosine Modifications in Double-Stranded DNA.ACS catalysis · 2022Article
- Structure and Function of TET Enzymes.Advances in experimental medicine and biology · 2022Article
- DNA Demethylation in the Processes of Repair and Epigenetic Regulation Performed by 2-Ketoglutarate-Dependent DNA Dioxygenases.International journal of molecular sciences · 2021Review
- TET-TDG Active DNA Demethylation at CpG and Non-CpG Sites.Journal of molecular biology · 2021Article
- Harnessing Alternative Substrates to Probe TET Family Enzymes.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Enzymatic Hydroxylation and Excision of Extended 5-Methylcytosine Analogues.Journal of molecular biology · 2020Article
- Nucleobase Modifiers Identify TET Enzymes as Bifunctional DNA Dioxygenases Capable of Direct N-Demethylation.Angewandte Chemie (International ed. in English) · 2020Article
- Site- and degree-specific C-H oxidation on 5-methylcytosine homologues for probing active DNA demethylation.Chemical science · 2019Article
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Authors and funding
4 authors.
Funding
Abstract
Ten-eleven translocation (TET) enzymes catalyze repeated oxidations of 5-methylcytosine in genomic DNA. Because of the challenges of tracking reactivity within a complex DNA substrate, chemical tools to probe TET activity are limited, despite these enzyme's crucial role in epigenetic regulation. Here, building on precedents from related Fe(II)/α-ketoglutarate-dependent dioxygenases, we show that TET enzymes can promiscuously act upon cytosine bases with unnatural 5-position modifications. Oxidation of 5-vinylcytosine (vC) in DNA results in the predominant formation of a 5-formylmethylcytosine product that can be efficiently labeled to provide an end-point read-out for TET activity. The reaction with 5-ethynylcytosine (eyC), moreover, results in the formation of a high-energy ketene intermediate that can selectively trap any active TET isoform as a covalent enzyme-DNA complex, even in the complex milieu of a total cell lysate. Exploiting substrate promiscuity therefore offers a new and needed means to directly track TET activity in vitro or in vivo.
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