ArticleNature structural & molecular biology2009
Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 81 citations in OpenAlex.
- Interprotomer communication and functional asymmetry in H/ACA snoRNPs.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Recent progress in human telomerase structure and its therapeutic targeting.Frontiers in molecular biosciences · 2025Review
- Landscape of RNA pseudouridylation in archaeon Sulfolobus islandicus.Nucleic acids research · 2024Article
- 2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein.Nature communications · 2024Article
- Improved Sampling of Adaptive Path Collective Variables by Stabilized Extended-System Dynamics.Journal of chemical theory and computation · 2023Article
- New faces of prokaryotic mobile genetic elements: guide RNAs link transposition with host defense mechanisms.Current opinion in systems biology · 2023Article
- Proteomic analyses reveal new features of the box H/ACA RNP biogenesis.Nucleic acids research · 2023Article
- The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1.PloS one · 2023Article
- Maturation of small nucleolar RNAs: from production to function.RNA biology · 2023Review
- CryoEM structures of pseudouridine-free ribosome suggest impacts of chemical modifications on ribosome conformations.Structure (London, England : 1993) · 2022Article
- Guide RNA acrobatics: positioning consecutive uridines for pseudouridylation by H/ACA pseudouridylation loops with dual guide capacity.Genes & development · 2022Article
- Dyskerin: an essential pseudouridine synthase with multifaceted roles in ribosome biogenesis, splicing, and telomere maintenance.RNA (New York, N.Y.) · 2021Review
- Structural dynamics govern substrate recruitment and catalytic turnover in H/ACA RNP pseudouridylation.RNA biology · 2021Article
- Eukaryote specific RNA and protein features facilitate assembly and catalysis of H/ACA snoRNPs.Nucleic acids research · 2021Article
- H/ACA Small Ribonucleoproteins: Structural and Functional Comparison Between Archaea and Eukaryotes.Frontiers in microbiology · 2021Review
- Pseudouridylation defect due toProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The presence of the ACA box in archaeal H/ACA guide RNAs promotes atypical pseudouridylation.RNA (New York, N.Y.) · 2020Article
- Contribution of protein Gar1 to the RNA-guided and RNA-independent rRNA:Ψ-synthase activities of the archaeal Cbf5 protein.Scientific reports · 2018Article
- The Role of scaRNAs in Adjusting Alternative mRNA Splicing in Heart Development.Journal of cardiovascular development and disease · 2018Review
- The Emerging Field of Epitranscriptomics in Neurodevelopmental and Neuronal Disorders.Frontiers in bioengineering and biotechnology · 2018Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Box H/ACA small nucleolar and Cajal body ribonucleoprotein particles comprise the most complex pseudouridine synthases and are essential for ribosome and spliceosome maturation. The multistep and multicomponent-mediated enzyme mechanism remains only partially understood. Here we report a crystal structure at 2.35 A of a substrate-bound functional archaeal enzyme containing three of the four proteins, Cbf5, Nop10 and L7Ae, and a box H/ACA RNA that reveals detailed information about the protein-only active site. The substrate RNA, containing 5-fluorouridine at the modification position, is fully docked and catalytically rearranged by the enzyme in a manner similar to that seen in two stand-alone pseudouridine synthases. Structural analysis provides a mechanism for plasticity in the diversity of guide RNA sequences used and identifies a substrate-anchoring loop of Cbf5 that also interacts with Gar1 in unliganded structures. Activity analyses of mutated proteins and RNAs support the structural findings and further suggest a role of the Cbf5 loop in regulation of enzyme activity.
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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.