ArticleNucleic acids research2019
Structural insights into a unique preference for 3' terminal guanine of mirtron in Drosophila TUTase 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 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- mirtronDB 2.0: enhanced database with novel mirtron discoveries.Bioinformatics (Oxford, England) · 2026Article
- Protonated Glutamate and Aspartate Side Chains Can Recognize Phosphodiester Groups via Strong and Short Hydrogen Bonds in Biomacromolecular Complexes.Angewandte Chemie (International ed. in English) · 2025Article
- Identification and Expression Analysis of the Nucleotidyl Transferase Protein (NTP) Family in Soybean (International journal of molecular sciences · 2024Article
- 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
- Regulation of angiogenesis by microRNAs in cancer.Molecular medicine reports · 2021Review
- Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases.Wiley interdisciplinary reviews. RNA · 2021Review
- Structure and mechanism of CutA, RNA nucleotidyl transferase with an unusual preference for cytosine.Nucleic acids research · 2020Article
- Revealing the hidden RBP-RNA interactions with RNA modification enzyme-based strategies.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Terminal uridylyl transferase (TUTase) is one type of enzyme that modifies RNA molecules by facilitating the post-transcriptional addition of uridyl ribonucleotides to their 3' ends. Recent researches have reported that Drosophila TUTase, Tailor, exhibits an intrinsic preference for RNA substrates ending in 3'G, distinguishing it from any other known TUTases. Through this unique feature, Tailor plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs. Here we describe crystal structures of core catalytic domain of Tailor and its complexes with RNA stretches 5'-AGU-3' and 5'-AGUU-3'. We demonstrate that R327 and N347 are two key residues contributing cooperatively to Tailor's preference for 3'G, and R327 may play an extra role in facilitating the extension of polyuridylation chain. We also demonstrate that conformational stability of the exit of RNA-binding groove also contributes significantly to Tailor's activity. Overall, our work reveals useful insights to explain why Drosophila Tailor can preferentially select RNA substrates ending in 3'G and provides important values for further understanding the biological significances of biogenesis pathway of mirtron in flies.
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