ArticleNucleic acids research2019
Structural basis for acceptor RNA substrate selectivity of the 3' terminal uridylyl transferase Tailor.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 10 citations in OpenAlex.
- Ashwin and FAM98 paralogs define nuclear and cytoplasmic RNA ligase complexes for tRNA biogenesis.Nature communications · 2026Article
- Intrinsic catalytic parameters drive specificity of non-templated poly(UG) tail synthesis.Nucleic acids research · 2026Article
- mirtronDB 2.0: enhanced database with novel mirtron discoveries.Bioinformatics (Oxford, England) · 2026Article
- Promiscuous splicing-derived hairpins are dominant substrates of tailing-mediated defense of miRNA biogenesis in mammals.Cell reports · 2023Article
- Molecular mechanism underlying the di-uridylation activity of Arabidopsis TUTase URT1.Nucleic acids research · 2022Article
- TENT2, TUT4, and TUT7 selectively regulate miRNA sequence and abundance.Nature communications · 2022Article
- Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases.Wiley interdisciplinary reviews. RNA · 2021Review
- Responsive fluorescent nucleotides serve as efficient substrates to probe terminal uridylyl transferase.Chemical communications (Cambridge, England) · 2020Article
- Structure and mechanism of CutA, RNA nucleotidyl transferase with an unusual preference for cytosine.Nucleic acids research · 2020Article
- Identification of Potential Inhibitors from Pyriproxyfen with Insecticidal Activity by Virtual Screening.Pharmaceuticals (Basel, Switzerland) · 2019Article
- Revealing the hidden RBP-RNA interactions with RNA modification enzyme-based strategies.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
5 authors at 2 institutions in 2 countries.
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Abstract
Non-templated 3'-uridylation of RNAs has emerged as an important mechanism for regulating the processing, stability and biological function of eukaryotic transcripts. In Drosophila, oligouridine tailing by the terminal uridylyl transferase (TUTase) Tailor of numerous RNAs induces their degradation by the exonuclease Dis3L2, which serves functional roles in RNA surveillance and mirtron RNA biogenesis. Tailor preferentially uridylates RNAs terminating in guanosine or uridine nucleotides but the structural basis underpinning its RNA substrate selectivity is unknown. Here, we report crystal structures of Tailor bound to a donor substrate analog or mono- and oligouridylated RNA products. These structures reveal specific amino acid residues involved in donor and acceptor substrate recognition, and complementary biochemical assays confirm the critical role of an active site arginine in conferring selectivity toward 3'-guanosine terminated RNAs. Notably, conservation of these active site features suggests that other eukaryotic TUTases, including mammalian TUT4 and TUT7, might exhibit similar, hitherto unknown, substrate selectivity. Together, these studies provide critical insights into the specificity of 3'-uridylation in eukaryotic post-transcriptional gene regulation.
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