Evidence map›Paper›PMID 30568249›Full record

ArticleNature communications2018

RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes.

Lukas Brüning, Philipp Hackert, Roman Martin, Jimena Davila Gallesio, Gerald Ryan R Aquino, Henning Urlaub, Katherine E Sloan, Markus T Bohnsack

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 44 citations in OpenAlex.

  1. Key Points to Consider When Studying RNA Remodeling by Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
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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 2 institutions in 1 country.

Lukas BrüningDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany.
Philipp HackertDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany.
Roman MartinDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany.
Jimena Davila GallesioDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany.
Gerald Ryan R AquinoDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany.
Henning UrlaubMax Planck Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry, 37077, Göttingen, Germany.
Katherine E SloanDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany. katherine.sloan@med.uni-goettingen.de.
Markus T BohnsackDepartment of Molecular Biology, University Medical Center Göttingen, 37073, Göttingen, Germany. markus.bohnsack@med.uni-goettingen.de.
University of Göttingen · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Production of eukaryotic ribosomal subunits is a highly dynamic process; pre-ribosomes undergo numerous structural rearrangements that establish the architecture present in mature complexes and serve as key checkpoints, ensuring the fidelity of ribosome assembly. Using in vivo crosslinking, we here identify the pre-ribosomal binding sites of three RNA helicases. Our data support roles for Has1 in triggering release of the U14 snoRNP, a critical event during early 40S maturation, and in driving assembly of domain I of pre-60S complexes. Binding of Mak5 to domain II of pre-60S complexes promotes recruitment of the ribosomal protein Rpl10, which is necessary for subunit joining and ribosome function. Spb4 binds to a molecular hinge at the base of ES27 facilitating binding of the export factor Arx1, thereby promoting pre-60S export competence. Our data provide important insights into the driving forces behind key structural remodelling events during ribosomal subunit assembly.

Indexed as

Adenosine TriphosphatasesBinding SitesDEAD-box RNA HelicasesRibosomal ProteinsRibosome SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesArx1 protein, S cerevisiaeDEAD-box RNA HelicasesHas1 protein, S cerevisiaeMAK5 protein, S cerevisiaeRibosomal ProteinsRPL10 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPB4 protein, S cerevisiae

Identifiers

PMID30568249
PMCPMC6300602
OpenAlexW2905082470

What OpenQuestion holds

Textmetadata
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.