ArticleBiochemistry2010
Functional and structural impact of target uridine substitutions on the H/ACA ribonucleoprotein particle pseudouridine synthase.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 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
- Mapping of pseudouridine residues on cellular and viral transcripts using a novel antibody-based technique.RNA (New York, N.Y.) · 2021Article
- Structural dynamics govern substrate recruitment and catalytic turnover in H/ACA RNP pseudouridylation.RNA biology · 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
- Structure-function relationships of archaeal Cbf5 during in vivo RNA-guided pseudouridylation.RNA (New York, N.Y.) · 2016Article
- Validation and correction of Zn-CysActa crystallographica. Section D, Structural biology · 2016Article
- Revisiting the structure/function relationships of H/ACA(-like) RNAs: a unified model for Euryarchaea and Crenarchaea.Nucleic acids research · 2015Article
- RNA-guided isomerization of uridine to pseudouridine--pseudouridylation.RNA biology · 2014Review
- FTO levels affect RNA modification and the transcriptome.European journal of human genetics : EJHG · 2013Article
- Article
- Kinetic and thermodynamic characterization of the reaction pathway of box H/ACA RNA-guided pseudouridine formation.Nucleic acids research · 2012Article
- Structures of ribonucleoprotein particle modification enzymes.Quarterly reviews of biophysics · 2011Review
- Posttranscriptional RNA Pseudouridylation.The EnzymesReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Box H/ACA ribonucleoprotein protein particles catalyze the majority of pseudouridylation in functional RNA. Different from stand alone pseudouridine synthases, the RNP pseudouridine synthase comprises multiple protein subunits and an RNA subunit. Previous studies showed that each subunit, regardless its location, is sensitive to the step of subunit placement at the catalytic center and potentially to the reaction status of the substrate. Here we describe the impact of chemical substitutions of target uridine on enzyme activity and structure. We found that 3-methyluridine in place of uridine inhibited its isomerization while 2'-deoxyuridine or 4-thiouridine did not. Significantly, crystal structures of an archaeal box H/ACA RNP bound with the nonreactive and the two postreactive substrate analogues showed only subtle structural changes throughout the assembly except for a conserved tyrosine and a substrate anchoring loop of Cbf5. Our results suggest a potential role of these elements and the subunit that contacts them in substrate binding and product release.
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