Evidence map›Paper›PMID 25535329›Full record

ArticleMolecular and cellular biology2015

DEAD-box RNA helicase Dbp4 is required for small-subunit processome formation and function.

Sahar Soltanieh, Yvonne N Osheim, Krasimir Spasov, Christian Trahan, Ann L Beyer, François Dragon

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

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  5. HumanFrontiers in genetics · 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

6 authors at 2 institutions in 2 countries.

Sahar SoltaniehDépartement des sciences biologiques and Centre de recherche BioMed, Université du Québec à Montréal, Montreal, Quebec, Canada.
Yvonne N OsheimDepartment of Microbiology, Immunology and Cancer Biology, University of Virginia Health System, Charlottesville, Virginia, USA.
Krasimir SpasovDépartement des sciences biologiques and Centre de recherche BioMed, Université du Québec à Montréal, Montreal, Quebec, Canada.
Christian TrahanDépartement des sciences biologiques and Centre de recherche BioMed, Université du Québec à Montréal, Montreal, Quebec, Canada.
Ann L BeyerDepartment of Microbiology, Immunology and Cancer Biology, University of Virginia Health System, Charlottesville, Virginia, USA.
François DragonDépartement des sciences biologiques and Centre de recherche BioMed, Université du Québec à Montréal, Montreal, Quebec, Canada dragon.francois@uqam.ca.
Université du Québec à Montréal · CAUniversity of Virginia Health System · US

Funding

Visualizing Genetic Activity in Normal & Mutant YeastR01GM063952 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI BEYER, ANN L. · 2001 to 2013
$3.7M
NIGMS NIH HHS R01 GM063952NIGMS NIH HHS R01GM063952
6 · The paper itself

Abstract

DEAD-box RNA helicase Dbp4 is required for 18S rRNA synthesis: cellular depletion of Dbp4 impairs the early cleavage reactions of the pre-rRNA and causes U14 small nucleolar RNA (snoRNA) to remain associated with pre-rRNA. Immunoprecipitation experiments (IPs) carried out with whole-cell extracts (WCEs) revealed that hemagglutinin (HA)-tagged Dbp4 is associated with U3 snoRNA but not with U14 snoRNA. IPs with WCEs also showed association with the U3-specific protein Mpp10, which suggests that Dbp4 interacts with the functionally active U3 RNP; this particle, called the small-subunit (SSU) processome, can be observed at the 5' end of nascent pre-rRNA. Electron microscopy analyses indicated that depletion of Dbp4 compromised SSU processome formation and cotranscriptional cleavage of the pre-rRNA. Sucrose density gradient analyses revealed that depletion of U3 snoRNA or the Mpp10 protein inhibited the release of U14 snoRNA from pre-rRNA, just as was seen with Dbp4-depleted cells, indicating that alteration of SSU processome components has significant consequences for U14 snoRNA dynamics. We also found that the C-terminal extension flanking the catalytic core of Dbp4 plays an important role in the release of U14 snoRNA from pre-rRNA.

Indexed as

Centrifugation, Density GradientChromatinDEAD-box RNA HelicasesGenotypeMicroscopy, ElectronPhosphoproteinsProtein Structure, TertiaryRibonucleoproteinsRibosomesRNA HelicasesRNA NucleotidyltransferasesRNA, Ribosomal, 18SRNA, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsChromatinDEAD-box RNA HelicasesHCA4 protein, S cerevisiaeMPP10 protein, S cerevisiaePhosphoproteinsRibonucleoproteinsRNA HelicasesRNA NucleotidyltransferasesRNA, Ribosomal, 18SRNA, Small NucleolarRNA, U3 small nucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID25535329
PMCPMC4323488
OpenAlexW1991350843

What OpenQuestion holds

Textmetadata
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.