Evidence map›Paper›PMID 15964797›Full record

ArticleMolecular and cellular biology2005

The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae.

Monica Ballarino, Mariangela Morlando, Francesca Pagano, Alessandro Fatica, Irene Bozzoni

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Splicing inactivation generates hybrid mRNA-snoRNA transcripts targeted by cytoplasmic RNA decay.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. The Existence and Localization of Nuclear snoRNAs inPlants (Basel, Switzerland) · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
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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

5 authors at 2 institutions in 1 country.

Monica BallarinoInstitute Pasteur Fondazione Cenci-Bolognetti, Department of Genetics and Molecular Biology, University La Sapienza, P.le A. Moro 5, 00185 Rome, Italy.
Mariangela Morlando
Francesca Pagano
Alessandro Fatica
Irene Bozzoni
Istituto Pasteur · ITInstitute of Molecular Biology and Pathology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The carboxy-terminal domain (CTD) of RNA polymerase II large subunit acts as a platform to assemble the RNA processing machinery in a controlled way throughout the transcription cycle. In yeast, recent findings revealed a physical connection between phospho-CTD, generated by the Ctk1p kinase, and protein factors having a function in small nucleolar RNA (snoRNA) biogenesis. The snoRNAs represent a large family of polymerase II noncoding transcripts that are associated with highly conserved polypeptides to form stable ribonucleoprotein particles (snoRNPs). In this work, we have studied the biogenesis of the snoRNPs belonging to the box H/ACA class. We report that the assembly factor Naf1p and the core components Cbf5p and Nhp2p are recruited on H/ACA snoRNA genes very early during transcription. We also show that the cotranscriptional recruitment of Naf1p and Cbf5p is Ctk1p dependent and that Ctk1p and Cbf5p are required for preventing the readthrough into the snoRNA downstream genes. All these data suggest that proper cotranscriptional snoRNP assembly controls 3'-end formation of snoRNAs and, consequently, the release of a functional particle.

Indexed as

Transcription, GeneticChromatin ImmunoprecipitationCyclinsFungal ProteinsHydro-LyasesMicrotubule-Associated ProteinsModels, MolecularNuclear ProteinsProtein KinasesReverse Transcriptase Polymerase Chain ReactionRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRNA, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCBF5 protein, S cerevisiaeCTDK-I protein complex, S cerevisiaeCyclinsFungal ProteinsHydro-LyasesMicrotubule-Associated ProteinsNuclear ProteinsProtein KinasesRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRNA, Small NucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID15964797
PMCPMC1156983
OpenAlexW2120837093

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.