ArticleNucleic acids research2012
Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
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- Accelerating primer design for amplicon sequencing using large language model-powered agents.Nature biomedical engineering · 2026Article
- Computational evolution of poly(U) polymerase for efficient and controlled RNA oligonucleotide synthesis.Nucleic acids research · 2026Article
- Gaussian Accelerated Molecular Dynamics Simulations Combined with NRIMD to Explore the Mechanism of Substrate Selectivity of Cid1 Polymerase for Different Nucleoside Triphosphates.International journal of molecular sciences · 2025Article
- Template-independent enzymatic synthesis of RNA oligonucleotides.Nature biotechnology · 2025Article
- Inducible auto-phosphorylation regulates a widespread family of nucleotidyltransferase toxins.Nature communications · 2024Article
- Structural basis for activity switching in polymerases determining the fate of let-7 pre-miRNAs.Nature structural & molecular biology · 2024Article
- Mechanism of U6 snRNA oligouridylation by human TUT1.Nature communications · 2023Article
- Molecular mechanism underlying the di-uridylation activity of Arabidopsis TUTase URT1.Nucleic acids research · 2022Article
- Nanocellulose Composites as Smart Devices With Chassis, Light-Directed DNA Storage, Engineered Electronic Properties, and Chip Integration.Frontiers in bioengineering and biotechnology · 2022Article
- Synthesis of modified nucleotide polymers by the poly(U) polymerase Cid1: application to direct RNA sequencing on nanopores.RNA (New York, N.Y.) · 2021Article
- 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
- A tale of non-canonical tails: gene regulation by post-transcriptional RNA tailing.Nature reviews. Molecular cell biology · 2020Review
- Terminal Uridylyl Transferase Mediated Site-Directed Access to Clickable Chromatin Employing CRISPR-dCas9.Journal of the American Chemical Society · 2020Article
- Gld2 activity is regulated by phosphorylation in the N-terminal domain.RNA biology · 2019Article
- Unbiased screen of RNA tailing activities reveals a poly(UG) polymerase.Nature methods · 2019Article
- Crystal structure of the Lin28-interacting module of human terminal uridylyltransferase that regulates let-7 expression.Nature communications · 2019Article
- RNA surveillance by uridylation-dependent RNA decay in Schizosaccharomyces pombe.Nucleic acids research · 2019Article
- Structural basis for acceptor RNA substrate selectivity of the 3' terminal uridylyl transferase Tailor.Nucleic acids research · 2019Article
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3 authors.
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Abstract
Polyuridylation is emerging as a ubiquitous post-translational modification with important roles in multiple aspects of RNA metabolism. These poly (U) tails are added by poly (U) polymerases with homology to poly (A) polymerases; nevertheless, the selection for UTP over ATP remains enigmatic. We report the structures of poly (U) polymerase Cid1 from Schizoscaccharomyces pombe alone and in complex with UTP, CTP, GTP and 3'-dATP. These structures reveal that each of the 4 nt can be accommodated at the active site; however, differences exist that suggest how the polymerase selects UTP over the other nucleotides. Furthermore, we find that Cid1 shares a number of common UTP recognition features with the kinetoplastid terminal uridyltransferases. Kinetic analysis of Cid1's activity for its preferred substrates, UTP and ATP, reveal a clear preference for UTP over ATP. Ultimately, we show that a single histidine in the active site plays a pivotal role for poly (U) activity. Notably, this residue is typically replaced by an asparagine residue in Cid1-family poly (A) polymerases. By mutating this histidine to an asparagine residue in Cid1, we diminished Cid1's activity for UTP addition and improved ATP incorporation, supporting that this residue is important for UTP selectivity.
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