Evidence map›Paper›PMID 34686661›Full record

ArticleNature communications2021

The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly.

Gerald Ryan R Aquino, Philipp Hackert, Nicolai Krogh, Kuan-Ting Pan, Mariam Jaafar, Anthony K Henras, Henrik Nielsen, Henning Urlaub, Katherine E Bohnsack, Markus T Bohnsack

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

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  12. A snoRNA-tRNA modification network governs codon-biased cellular states.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

10 authors.

Gerald Ryan R AquinoDepartment of Molecular Biology, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.ORCID 0000-0003-2536-839X
Philipp HackertDepartment of Molecular Biology, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.
Nicolai KroghDepartment of Cellular and Molecular Medicine, University of Copenhagen, 2200N, Copenhagen, Denmark.
Kuan-Ting PanMax Planck Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry, 37077, Göttingen, Germany.ORCID 0000-0001-6974-5324
Mariam JaafarMolecular, Cellular and Developmental Biology Unit (MCD), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, 31062, Toulouse, France.
Anthony K HenrasMolecular, Cellular and Developmental Biology Unit (MCD), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, 31062, Toulouse, France.ORCID 0000-0001-7785-9938
Henrik NielsenDepartment of Cellular and Molecular Medicine, University of Copenhagen, 2200N, Copenhagen, Denmark.ORCID 0000-0001-7143-2810
Henning UrlaubMax Planck Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry, 37077, Göttingen, Germany.ORCID 0000-0003-1837-5233
Katherine E BohnsackDepartment of Molecular Biology, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany. katherine.bohnsack@med.uni-goettingen.de.ORCID 0000-0001-6035-4255
Markus T BohnsackDepartment of Molecular Biology, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany. markus.bohnsack@med.uni-goettingen.de.ORCID 0000-0001-7063-5456

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5' and 3' ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation.

Indexed as

Adenosine TriphosphatasesDEAD-box RNA HelicasesMolecular ChaperonesNuclear ProteinsRibosomal Protein L3Ribosome Subunits, Large, EukaryoticRNA FoldingRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, RibosomalRNA, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesDBP7 protein, S cerevisiaeDEAD-box RNA HelicasesMolecular ChaperonesNuclear ProteinsRibosomal Protein L3RNA-dependent ATPaseRNA PrecursorsRNA, RibosomalRNA, ribosomal, 25SRNA, Small NucleolarSaccharomyces cerevisiae ProteinsURB1 protein, S cerevisiae

Identifiers

PMID34686661
PMCPMC8536713

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Registered trials

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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.