Evidence map›Paper›PMID 27530427›Full record

ArticleNucleic acids research2016

Structure of a human pre-40S particle points to a role for RACK1 in the final steps of 18S rRNA processing.

Natacha Larburu, Christian Montellese, Marie-Françoise O'Donohue, Ulrike Kutay, Pierre-Emmanuel Gleizes, Célia Plisson-Chastang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 49 citations in OpenAlex.

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  18. RACK1 on and off the ribosome.RNA (New York, N.Y.) · 2019
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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

6 authors at 5 institutions in 2 countries.

Natacha LarburuLaboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative, Université de Toulouse, CNRS, UPS, France.
Christian MontelleseInstitut für Biochemie, ETH Zürich, CH-8093 Zurich, Switzerland.
Marie-Françoise O'DonohueLaboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative, Université de Toulouse, CNRS, UPS, France.
Ulrike KutayInstitut für Biochemie, ETH Zürich, CH-8093 Zurich, Switzerland.
Pierre-Emmanuel GleizesLaboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative, Université de Toulouse, CNRS, UPS, France gleizes@ibcg.biotoul.fr.
Célia Plisson-ChastangLaboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative, Université de Toulouse, CNRS, UPS, France plisson@ibcg.biotoul.fr.
ETH Zurich · CHCentre National de la Recherche Scientifique · FRLaboratoire de Biologie Moléculaire des Eucaryotes · FRUniversité Fédérale de Toulouse Midi-Pyrénées · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synthesis of ribosomal subunits in eukaryotes is a complex and tightly regulated process that has been mostly characterized in yeast. The discovery of a growing number of diseases linked to defects in ribosome biogenesis calls for a deeper understanding of these mechanisms and of the specificities of human ribosome maturation. We present the 19 Å resolution cryo-EM reconstruction of a cytoplasmic precursor to the human small ribosomal subunit, purified by using the tagged ribosome biogenesis factor LTV1 as bait. Compared to yeast pre-40S particles, this first three-dimensional structure of a human 40S subunit precursor shows noticeable differences with respect to the position of ribosome biogenesis factors and uncovers the early deposition of the ribosomal protein RACK1 during subunit maturation. Consistently, RACK1 is required for efficient processing of the 18S rRNA 3'-end, which might be related to its role in translation initiation. This first structural analysis of a human pre-ribosomal particle sets the grounds for high-resolution studies of conformational transitions accompanying ribosomal subunit maturation.

Indexed as

Conserved SequenceCryoelectron MicroscopyCytoplasmGTP-Binding ProteinsHEK293 CellsHeLa CellsHumansModels, MolecularNeoplasm ProteinsOrganelle BiogenesisProtein BindingReceptors, Cell SurfaceReceptors for Activated C KinaseRibosomal ProteinsRibosome Subunits, Small, EukaryoticRNA Processing, Post-TranscriptionalGTP-Binding ProteinsNeoplasm ProteinsRACK1 protein, humanReceptors, Cell SurfaceReceptors for Activated C KinaseRibosomal ProteinsRNA, Ribosomal, 18S

Identifiers

PMID27530427
PMCPMC5041492
OpenAlexW2517092495

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.