Evidence map›Paper›PMID 36018804›Full record

ArticleNucleic acids research2022

Rbp95 binds to 25S rRNA helix H95 and cooperates with the Npa1 complex during early pre-60S particle maturation.

Priya Bhutada, Sébastien Favre, Mariam Jaafar, Jutta Hafner, Laura Liesinger, Stefan Unterweger, Karin Bischof, Barbara Darnhofer, Devanarayanan Siva Sankar, Gerald Rechberger and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

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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

16 authors at 6 institutions in 4 countries.

Priya BhutadaInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Sébastien FavreUnit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.
Mariam JaafarMolecular, Cellular and Developmental Biology Unit (MCD), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, 31062 Toulouse, France.
Jutta HafnerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Laura LiesingerBioTechMed-Graz, Graz, Austria.
Stefan UnterwegerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Karin BischofInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Barbara DarnhoferBioTechMed-Graz, Graz, Austria.
Devanarayanan Siva SankarUnit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.
Gerald RechbergerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Raghida Abou MerhiGenomic Stability and Biotherapy (GSBT) Laboratory, Faculty of Sciences, Rafik Hariri Campus, Lebanese University, Beirut, Lebanon.
Simon LebaronMolecular, Cellular and Developmental Biology Unit (MCD), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, 31062 Toulouse, France.
Ruth Birner-GruenbergerBioTechMed-Graz, Graz, Austria.
Dieter KresslerUnit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.
Anthony K HenrasMolecular, Cellular and Developmental Biology Unit (MCD), Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, 31062 Toulouse, France.
Brigitte PertschyInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.ORCID 0000-0003-3558-0191
University of Graz · ATCentre National de la Recherche Scientifique · FRUniversity of Fribourg · CHMedical University of Graz · ATLebanese University · LBTU Wien · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic ribosome synthesis involves more than 200 assembly factors, which promote ribosomal RNA (rRNA) processing, modification and folding, and assembly of ribosomal proteins. The formation and maturation of the earliest pre-60S particles requires structural remodeling by the Npa1 complex, but is otherwise still poorly understood. Here, we introduce Rbp95 (Ycr016w), a constituent of early pre-60S particles, as a novel ribosome assembly factor. We show that Rbp95 is both genetically and physically linked to most Npa1 complex members and to ribosomal protein Rpl3. We demonstrate that Rbp95 is an RNA-binding protein containing two independent RNA-interacting domains. In vivo, Rbp95 associates with helix H95 in the 3' region of the 25S rRNA, in close proximity to the binding sites of Npa1 and Rpl3. Additionally, Rbp95 interacts with several snoRNAs. The absence of Rbp95 results in alterations in the protein composition of early pre-60S particles. Moreover, combined mutation of Rbp95 and Npa1 complex members leads to a delay in the maturation of early pre-60S particles. We propose that Rbp95 acts together with the Npa1 complex during early pre-60S maturation, potentially by promoting pre-rRNA folding events within pre-60S particles.

Indexed as

Ribosome Subunits, Large, EukaryoticNuclear ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA PrecursorsRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsNuclear ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA PrecursorsRNA, RibosomalRNA, ribosomal, 25SSaccharomyces cerevisiae ProteinsURB1 protein, S cerevisiae

Identifiers

PMID36018804
PMCPMC9508819
OpenAlexW4293149151

What OpenQuestion holds

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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.