Evidence map›Paper›PMID 24823650›Full record

ArticlePLoS biology2014

RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.

Jérôme Loc'h, Magali Blaud, Stéphane Réty, Simon Lebaron, Patrick Deschamps, Joseph Bareille, Julie Jombart, Julien Robert-Paganin, Lila Delbos, Florian Chardon and 4 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

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  15. Eukaryotic ribosome assembly, transport and quality control.Nature structural & molecular biology · 2017
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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

14 authors at 5 institutions in 2 countries.

Jérôme Loc'hLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Magali BlaudLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Stéphane RétyLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Simon LebaronLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France; Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, Scotland.
Patrick DeschampsLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Joseph BareilleLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Julie JombartLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Julien Robert-PaganinLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Lila DelbosLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Florian ChardonLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Elodie ZhangLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Clément CharentonLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
David TollerveyWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, Scotland.
Nicolas LeulliotLaboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Faculté de Pharmacie, Sorbonne Paris Cité, Paris, France.
Centre National de la Recherche Scientifique · FRUniversité Paris Cité · FRLaboratoire de Cristallographie et RMN Biologiques · FRSorbonne Paris Cité · FRWellcome Centre for Cell Biology · GB

Funding

Wellcome Trust 077248Wellcome Trust 092076
6 · The paper itself

Abstract

During biogenesis of the 40S and 60S ribosomal subunits, the pre-40S particles are exported to the cytoplasm prior to final cleavage of the 20S pre-rRNA to mature 18S rRNA. Amongst the factors involved in this maturation step, Fap7 is unusual, as it both interacts with ribosomal protein Rps14 and harbors adenylate kinase activity, a function not usually associated with ribonucleoprotein assembly. Human hFap7 also regulates Cajal body assembly and cell cycle progression via the p53-MDM2 pathway. This work presents the functional and structural characterization of the Fap7-Rps14 complex. We report that Fap7 association blocks the RNA binding surface of Rps14 and, conversely, Rps14 binding inhibits adenylate kinase activity of Fap7. In addition, the affinity of Fap7 for Rps14 is higher with bound ADP, whereas ATP hydrolysis dissociates the complex. These results suggest that Fap7 chaperones Rps14 assembly into pre-40S particles via RNA mimicry in an ATP-dependent manner. Incorporation of Rps14 by Fap7 leads to a structural rearrangement of the platform domain necessary for the pre-rRNA to acquire a cleavage competent conformation.

Indexed as

Gene Expression Regulation, FungalAdenosine DiphosphateAdenosine TriphosphateAdenylate KinaseAmino Acid SequenceEscherichia coliHumansModels, MolecularMolecular MimicryMolecular Sequence DataNuclear ProteinsNucleoside-TriphosphatasePyrococcus abyssiRecombinant ProteinsRibosomal ProteinsRibosome Subunits, Large, EukaryoticAdenosine DiphosphateAdenosine TriphosphateAdenylate KinaseFAP7 protein, S cerevisiaeNuclear ProteinsNucleoside-TriphosphataseRecombinant ProteinsRibosomal ProteinsRNA, Ribosomal, 18SRPS14A protein, S cerevisiaeRPS14B protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID24823650
PMCPMC4019466
OpenAlexW2070653865

What OpenQuestion holds

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LicenceCC BY
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.