ArticleNucleic acids research2014
A critical switch in the enzymatic properties of the Cid1 protein deciphered from its product-bound crystal structure.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- 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
- Molecular mechanism underlying the di-uridylation activity of Arabidopsis TUTase URT1.Nucleic acids research · 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
- 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
- Terminal Uridylyl Transferase Mediated Site-Directed Access to Clickable Chromatin Employing CRISPR-dCas9.Journal of the American Chemical Society · 2020Article
- aBravo Is a NovelViruses · 2020Article
- 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
- Structural insights into a unique preference for 3' terminal guanine of mirtron in Drosophila TUTase tailor.Nucleic acids research · 2019Article
- Function and Regulation of Human Terminal Uridylyltransferases.Frontiers in genetics · 2018Review
- Biochemical and structural bioinformatics studies of fungal CutA nucleotidyltransferases explain their unusual specificity toward CTP and increased tendency for cytidine incorporation at the 3'-terminal positions of synthesized tails.RNA (New York, N.Y.) · 2017Article
- Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.Nature structural & molecular biology · 2017Article
- Crystal structures of U6 snRNA-specific terminal uridylyltransferase.Nature communications · 2017Article
- RNA Editing TUTase 1: structural foundation of substrate recognition, complex interactions and drug targeting.Nucleic acids research · 2016Article
- Structural basis for the activation of the C. elegans noncanonical cytoplasmic poly(A)-polymerase GLD-2 by GLD-3.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural plasticity of Cid1 provides a basis for its distributive RNA terminal uridylyl transferase activity.Nucleic acids research · 2015Article
- Improved crystallization and diffraction of caffeine-induced death suppressor protein 1 (Cid1).Acta crystallographica. Section F, Structural biology communications · 2015Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The addition of uridine nucleotide by the poly(U) polymerase (PUP) enzymes has a demonstrated impact on various classes of RNAs such as microRNAs (miRNAs), histone-encoding RNAs and messenger RNAs. Cid1 protein is a member of the PUP family. We solved the crystal structure of Cid1 in complex with non-hydrolyzable UMPNPP and a short dinucleotide compound ApU. These structures revealed new residues involved in substrate/product stabilization. In particular, one of the three catalytic aspartate residues explains the RNA dependence of its PUP activity. Moreover, other residues such as residue N165 or the β-trapdoor are shown to be critical for Cid1 activity. We finally suggest that the length and sequence of Cid1 substrate RNA influence the balance between Cid1's processive and distributive activities. We propose that particular processes regulated by PUPs require the enzymes to switch between the two types of activity as shown for the miRNA biogenesis where PUPs can either promote DICER cleavage via short U-tail or trigger miRNA degradation by adding longer poly(U) tail. The enzymatic properties of these enzymes may be critical for determining their particular function in vivo.
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