ArticleNucleic acids research2015
Structural plasticity of Cid1 provides a basis for its distributive RNA terminal uridylyl transferase activity.
Article in Nucleic acids research, 2015. 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.
- Structural basis for activity switching in polymerases determining the fate of let-7 pre-miRNAs.Nature structural & molecular biology · 2024Article
- 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
- 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
- Normal Mode Analysis as a Routine Part of a Structural Investigation.Molecules (Basel, Switzerland) · 2019Review
- Gld2 activity is regulated by phosphorylation in the N-terminal domain.RNA biology · 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
- 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
- 3' RNA Uridylation in Epitranscriptomics, Gene Regulation, and Disease.Frontiers in molecular biosciences · 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
- Structure of mitochondrial poly(A) RNA polymerase reveals the structural basis for dimerization, ATP selectivity and the SPAX4 disease phenotype.Nucleic acids research · 2015Article
- 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
- TUT7 controls the fate of precursor microRNAs by using three different uridylation mechanisms.The EMBO journal · 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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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Terminal uridylyl transferases (TUTs) are responsible for the post-transcriptional addition of uridyl residues to RNA 3' ends, leading in some cases to altered stability. The Schizosaccharomyces pombe TUT Cid1 is a model enzyme that has been characterized structurally at moderate resolution and provides insights into the larger and more complex mammalian TUTs, ZCCHC6 and ZCCHC11. Here, we report a higher resolution (1.74 Å) crystal structure of Cid1 that provides detailed evidence for uracil selection via the dynamic flipping of a single histidine residue. We also describe a novel closed conformation of the enzyme that may represent an intermediate stage in a proposed product ejection mechanism. The structural insights gained, combined with normal mode analysis and biochemical studies, demonstrate that the plasticity of Cid1, particularly about a hinge region (N164-N165), is essential for catalytic activity, and provide an explanation for its distributive uridylyl transferase activity. We propose a model clarifying observed differences between the in vitro apparently processive activity and in vivo distributive monouridylylation activity of Cid1. We suggest that modulating the flexibility of such enzymes-for example by the binding of protein co-factors-may allow them alternatively to add single or multiple uridyl residues to the 3' termini of RNA molecules.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.