Evidence map›Paper›PMID 12682021›Full record

ArticleThe EMBO journal2003

Pseudouridylation (Psi) of U2 snRNA in S. cerevisiae is catalyzed by an RNA-independent mechanism.

Xiaoju Ma, Xinliang Zhao, Yi-Tao Yu

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
4.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

73 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. tRNA pseudouridine synthase D (TruD) fromRNA (New York, N.Y.) · 2025
    Article
  5. Article
  6. Article
  7. Predicting Pseudouridine Sites with Porpoise.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. International journal of molecular sciences · 2021
    Review
  16. A single mNature communications · 2021
    Article
  17. Spliceosomal snRNA Epitranscriptomics.Frontiers in genetics · 2021
    Review
  18. Article
  19. Review
  20. Article

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Xiaoju MaDepartment of Biochemistry and Biophysics, University of Rochester Medical Center, 601 Elmwood Avenue, Rochester, NY 14642, USA.
Xinliang Zhao
Yi-Tao Yu
University of Rochester Medical Center · US

Funding

Spliceosomal snRNA modification in Xenopus oocytesR01GM062937 · NIGMS · UNIVERSITY OF ROCHESTER · PI YU, YI-TAO · 2001 to 2009
$2.3M
NIGMS NIH HHS GM62937NIGMS NIH HHS R01 GM062937
6 · The paper itself

Abstract

Pseudouridylation of snRNAs in vertebrates is guided by small nucleolar/Cajal body-specific RNAs (sno/scaRNAs). We developed an in vitro system using cell extracts and single site-radiolabeled U2 snRNAs to study pseudouridylation in Saccharomyces cerevisiae. Micrococcal nuclease-treated cell extracts are fully competent to catalyze U2 pseudouridylation, suggesting an RNA-independent process. A pseudouridylase activity for Psi(35) within yeast U2 is identified via a screen of an S.cerevisiae GST-ORF protein library. This activity is associated with YOR243c ORF, which has not previously been assigned function. When the GST-YOR243c protein is expressed in Escherichia coli, pseudouridylation activity is comparable to that expressed in S.cerevisiae, demonstrating that this protein (designated Pus7) alone can catalyze Psi(35) formation in U2. Both in vitro and in vivo analyses using wild-type and pus7-Delta strains show that Pus7 is indispensable for Psi(35) formation in U2. Using site-specific radiolabeled U2 and U2 fragments, we show that Pus7 activity is specific for Psi(35) and that the U2 stem- loop II region is essential for the pseudouridylation reaction. A BLAST search revealed Pus7 homologs in various organisms.

Indexed as

Amino Acid SequenceAnimalsBase SequenceGene LibraryGenes, ReporterMolecular Sequence DataNucleic Acid ConformationOpen Reading FramesRecombinant Fusion ProteinsRNA, Small NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentUridine Monophosphatepseudouridylic acidPus7 protein, S cerevisiaeRecombinant Fusion ProteinsRNA, Small NuclearSaccharomyces cerevisiae ProteinsU2 small nuclear RNAUridine Monophosphate

Identifiers

PMID12682021
PMCPMC154481
OpenAlexW2017942151

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.