Evidence map›Paper›PMID 26159998›Full record

ArticleGenes & development2015

Chaperoning 5S RNA assembly.

Clément Madru, Simon Lebaron, Magali Blaud, Lila Delbos, Juliana Pipoli, Eric Pasmant, Stéphane Réty, Nicolas Leulliot

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
–field-weighted citation impact
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

46 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Inherited human TFIIIA deficiency disrupts T cell development.medRxiv : the preprint server for health sciences · 2026
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  4. RNA Structure Coordinates Translation Across the Meiotic Program.bioRxiv : the preprint server for biology · 2026
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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

8 authors at 6 institutions in 1 country.

Clément MadruLaboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
Simon LebaronLaboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France; CR2 INSERM;
Magali BlaudLaboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
Lila DelbosLaboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
Juliana PipoliPlateforme Génomique, Institut Cochin, UMR_S1016, INSERM, 75006 Paris, France;
Eric PasmantService de Biochimie et Génétique Moléculaire, Hôpital Cochin, Assistance Publique-Hôpitaux de Paris, 75006 Paris, France.
Stéphane RétyLaboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
Nicolas LeulliotLaboratoire de Cristallographie et RMN Biologiques, UMR, CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, 75006 Paris, France;
Sorbonne Paris Cité · FRUniversité Paris Cité · FRCentre National de la Recherche Scientifique · FRHôpital Cochin · FRInstitut Cochin · FRLaboratoire de Cristallographie et RMN Biologiques · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, three of the four ribosomal RNAs (rRNAs)—the 5.8S, 18S, and 25S/28S rRNAs—are processed from a single pre-rRNA transcript and assembled into ribosomes. The fourth rRNA, the 5S rRNA, is transcribed by RNA polymerase III and is assembled into the 5S ribonucleoprotein particle (RNP), containing ribosomal proteins Rpl5/uL18 and Rpl11/uL5, prior to its incorporation into preribosomes. In mammals, the 5S RNP is also a central regulator of the homeostasis of the tumor suppressor p53. The nucleolar localization of the 5S RNP and its assembly into preribosomes are performed by a specialized complex composed of Rpf2 and Rrs1 in yeast or Bxdc1 and hRrs1 in humans. Here we report the structural and functional characterization of the Rpf2-Rrs1 complex alone, in complex with the 5S RNA, and within pre-60S ribosomes. We show that the Rpf2-Rrs1 complex contains a specialized 5S RNA E-loop-binding module, contacts the Rpl5 protein, and also contacts the ribosome assembly factor Rsa4 and the 25S RNA. We propose that the Rpf2-Rrs1 complex establishes a network of interactions that guide the incorporation of the 5S RNP in preribosomes in the initial conformation prior to its rotation to form the central protuberance found in the mature large ribosomal subunit.

Indexed as

Models, MolecularBinding SitesCryoelectron MicroscopyNuclear ProteinsProtein BindingProtein Structure, QuaternaryRNA-Binding ProteinsRNA, Ribosomal, 5SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsNuclear ProteinsRNA-Binding ProteinsRNA, Ribosomal, 5SRPF2 protein, S cerevisiaeRRS1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins5S RNPBrix domainp53ribosome assembly

Identifiers

PMID26159998
PMCPMC4511217
OpenAlexW1869742654

What OpenQuestion holds

Textmetadata
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.