Evidence map›Paper›PMID 25064857›Full record

ArticleNucleic acids research2014

Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing.

Anna Delprato, Yasmine Al Kadri, Natacha Pérébaskine, Cécile Monfoulet, Yves Henry, Anthony K Henras, Sébastien Fribourg

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  12. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  13. Article
  14. Review
  15. The complete structure of the small-subunit processome.Nature structural & molecular biology · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Anna DelpratoInstitut Européen de Chimie et Biologie, ARNA laboratory, Université de Bordeaux, F-33607 Pessac, France Institut National de la Santé Et de la Recherche Médicale, INSERM - U869, ARNA laboratory, F-33000 Bordeaux, France.
Yasmine Al KadriEquipe labellisée Ligue Contre le Cancer, Centre National de la Recherche Scientifique, Laboratoire de Biologie Moléculaire Eucaryote and Université de Toulouse, UPS, F-31062 Toulouse Cedex 9, France.
Natacha PérébaskineInstitut Européen de Chimie et Biologie, ARNA laboratory, Université de Bordeaux, F-33607 Pessac, France Institut National de la Santé Et de la Recherche Médicale, INSERM - U869, ARNA laboratory, F-33000 Bordeaux, France.
Cécile MonfouletInstitut Européen de Chimie et Biologie, ARNA laboratory, Université de Bordeaux, F-33607 Pessac, France Institut National de la Santé Et de la Recherche Médicale, INSERM - U869, ARNA laboratory, F-33000 Bordeaux, France.
Yves HenryEquipe labellisée Ligue Contre le Cancer, Centre National de la Recherche Scientifique, Laboratoire de Biologie Moléculaire Eucaryote and Université de Toulouse, UPS, F-31062 Toulouse Cedex 9, France.
Anthony K HenrasEquipe labellisée Ligue Contre le Cancer, Centre National de la Recherche Scientifique, Laboratoire de Biologie Moléculaire Eucaryote and Université de Toulouse, UPS, F-31062 Toulouse Cedex 9, France anthony.henras@ibcg.biotoul.fr.
Sébastien FribourgInstitut Européen de Chimie et Biologie, ARNA laboratory, Université de Bordeaux, F-33607 Pessac, France Institut National de la Santé Et de la Recherche Médicale, INSERM - U869, ARNA laboratory, F-33000 Bordeaux, France sebastien.fribourg@inserm.fr.ORCID http://orcid.org/0000-0003-4112-7510
Université de Bordeaux · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The essential Rcl1p and Bms1p proteins form a complex required for 40S ribosomal subunit maturation. Bms1p is a GTPase and Rcl1p has been proposed to catalyse the endonucleolytic cleavage at site A2 separating the pre-40S and pre-60S maturation pathways. We determined the 2.0 Å crystal structure of Bms1p associated with Rcl1p. We demonstrate that Rcl1p nuclear import depends on Bms1p and that the two proteins are loaded into pre-ribosomes at a similar stage of the maturation pathway and remain present within pre-ribosomes after cleavage at A2. Importantly, GTP binding to Bms1p is not required for the import in the nucleus nor for the incorporation of Rcl1p into pre-ribosomes, but is essential for early pre-rRNA processing. We propose that GTP binding to Bms1p and/or GTP hydrolysis may induce conformational rearrangements within the Bms1p-Rcl1p complex allowing the interaction of Rcl1p with its RNA substrate.

Indexed as

RNA Processing, Post-TranscriptionalActive Transport, Cell NucleusCell NucleusGene Expression Regulation, FungalGTP-Binding ProteinsGuanosine TriphosphateNuclear ProteinsPoint MutationProtein BindingProtein Interaction Domains and MotifsRibosomesRNA-Binding ProteinsRNA PrecursorsRNA, RibosomalSaccharomyces cerevisiae ProteinsBms1 protein, S cerevisiaeGTP-Binding ProteinsGuanosine TriphosphateNuclear ProteinsRCL1 protein, S cerevisiaeRNA-Binding ProteinsRNA PrecursorsRNA, RibosomalSaccharomyces cerevisiae Proteins

Identifiers

PMID25064857
PMCPMC4150785
OpenAlexW2052901000

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.