Evidence map›Paper›PMID 24234454›Full record

ArticleNucleic acids research2014

Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly.

Benjamin Rothé, Régis Back, Marc Quinternet, Jonathan Bizarro, Marie-Cécile Robert, Magali Blaud, Christophe Romier, Xavier Manival, Bruno Charpentier, Edouard Bertrand and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
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  11. The cellular landscape of mid-size noncoding RNA.Wiley interdisciplinary reviews. RNA · 2019
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  20. Noncoding RNAs in eukaryotic ribosome biogenesis and function.Nature structural & molecular biology · 2015
    Review
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

11 authors at 7 institutions in 2 countries.

Benjamin RothéIngénierie Moléculaire et Physiopathologie Articulaire (IMoPA), UMR 7365 CNRS Université de Lorraine, Biopôle de l'Université de Lorraine, Campus Biologie Santé, 9 avenue de la forêt de Haye, BP 184, 54505 Vandœuvre-lès-Nancy, France, FR CNRS-3209 (Ingénierie Moléculaire et Thérapeutique), CNRS, Université de Lorraine, Faculté de Médecine, Bâtiment Biopôle, BP 184, 54505 Vandœuvre-lès-Nancy Cedex, France, Equipe labellisée Ligue contre le Cancer, IGMM (Institut de Génétique Moléculaire de Montpellier), Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5535, Montpellier Cedex 5, France and IGBMC (Institut de Génétique et Biologie Moléculaire et Cellulaire), Département de Biologie et Génomique Structurales, Université de Strasbourg, CNRS, INSERM, 1 Rue Laurent Fries, BP 10142, 67404 Illkirch Cedex, France.
Régis Back
Marc Quinternet
Jonathan Bizarro
Marie-Cécile Robert
Magali Blaud
Christophe Romier
Xavier Manival
Bruno Charpentier
Edouard Bertrand
Christiane Branlant
Ingénierie Moléculaire et Physiopathologie Articulaire · FRCentre National de la Recherche Scientifique · FRÉcole Polytechnique Fédérale de Lausanne · CHInstitut de Biologie Moléculaire et Cellulaire · FRInstitut de Génétique Moléculaire de Montpellier · FRLa Ligue Contre le Cancer · FRUniversité de Lorraine · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast Snu13p protein and its 15.5K human homolog both bind U4 snRNA and box C/D snoRNAs. They also bind the Rsa1p/NUFIP assembly factor, proposed to scaffold immature snoRNPs and to recruit the Hsp90-R2TP chaperone complex. However, the nature of the Snu13p/15.5K-Rsa1p/NUFIP interaction and its exact role in snoRNP assembly remained to be elucidated. By using biophysical, molecular and imaging approaches, here, we identify residues needed for Snu13p/15.5K-Rsa1p/NUFIP interaction. By NMR structure determination and docking approaches, we built a 3D model of the Snup13p-Rsa1p interface, suggesting that residues R249, R246 and K250 in Rsa1p and E72 and D73 in Snu13p form a network of electrostatic interactions shielded from the solvent by hydrophobic residues from both proteins and that residue W253 of Rsa1p is inserted in a hydrophobic cavity of Snu13p. Individual mutations of residues in yeast demonstrate the functional importance of the predicted interactions for both cell growth and snoRNP formation. Using archaeal box C/D sRNP 3D structures as templates, the association of Snu13p with Rsa1p is predicted to be exclusive of interactions in active snoRNPs. Rsa1p and NUFIP may thus prevent premature activity of pre-snoRNPs, and their removal may be a key step for active snoRNP production.

Indexed as

Amino Acid SequenceHumansHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular ChaperonesMolecular Sequence DataNuclear ProteinsProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRibosomal ProteinsRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMolecular ChaperonesNuclear ProteinsPIH1 protein, S cerevisiaeRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRibosomal ProteinsRSA1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSnu13 protein, humanSnu13 protein, S cerevisiaeTah1 protein, S cerevisiae

Identifiers

PMID24234454
PMCPMC3919607
OpenAlexW2131565488

What OpenQuestion holds

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LicenceCC BY-NC
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.