Evidence map›Paper›PMID 16931875›Full record

ArticleRNA (New York, N.Y.)2006

Analysis of the binding of the N-terminal conserved domain of yeast Cbf5p to a box H/ACA snoRNA.

Christophe Normand, Regine Capeyrou, Sophie Quevillon-Cheruel, Annie Mougin, Yves Henry, Michele Caizergues-Ferrer

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. The fungal snoRNAome.RNA (New York, N.Y.) · 2018
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
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

6 authors at 3 institutions in 1 country.

Christophe NormandEquipe Labellisée Ligue Nationale contre le Cancer, Laboratoire de Biologie Moléculaire Eucaryote, UMR5099, CNRS-Université Paul Sabatier, IFR 109, Toulouse, France, European Union.
Regine Capeyrou
Sophie Quevillon-Cheruel
Annie Mougin
Yves Henry
Michele Caizergues-Ferrer
Laboratoire de Biologie Moléculaire des Eucaryotes · FRCentre National de la Recherche Scientifique · FRInstitut de Biochimie et Biophysique Moléculaire et Cellulaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During ribosome biogenesis, the RNA precursor to mature rRNAs undergoes numerous post-transcriptional chemical modifications of bases, including conversions of uridines to pseudouridines. In archaea and eukaryotes, these conversions are performed by box H/ACA small ribonucleoprotein particles (box H/ACA RNPs), which contain a small guide RNA responsible for the selection of substrate uridines and four proteins, including the pseudouridine synthase, Cbf5p. So far, no in vitro reconstitution of eukaryotic box H/ACA RNPs from purified components has been achieved, principally due to difficulties in purifying recombinant eukaryotic Cbf5p. In this study, we present the purification of a truncated derivative of yeast Cbf5p (Cbf5(Delta)p) that retains the highly conserved TRUB and PUA domains. We have used band retardation assays to show that Cbf5(Delta)p on its own binds to box H/ACA small nucleolar (sno)RNAs. We demonstrate that the conserved H and ACA boxes enhance the affinity of the protein for the snoRNA. Furthermore, like its archaeal homologs, Cbf5(Delta)p can bind to a single stem-loop-box ACA RNA. Finally, we report the first enzymatic footprinting analysis of a Cbf5-RNA complex. Our results are compatible with the view that two molecules of Cbf5p interact with a binding platform constituted by the 5' end of the RNA, the single-stranded hinge domain containing the conserved H box, and the 3' end of the molecule, including the conserved ACA box.

Indexed as

Amino Acid SequenceBase SequenceBinding SitesConserved SequenceHydro-LyasesMicrotubule-Associated ProteinsMolecular Sequence DataNucleic Acid ConformationProtein BindingProtein FootprintingProtein Structure, TertiaryRecombinant ProteinsRibonucleasesRibonucleoproteins, Small NuclearRNA, FungalRNA, Small NucleolarCBF5 protein, S cerevisiaeHydro-LyasesMicrotubule-Associated ProteinsRecombinant ProteinsRibonucleasesRibonucleoproteins, Small NuclearRNA, FungalRNA, Small NucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID16931875
PMCPMC1581976
OpenAlexW2169847445

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.