Evidence map›Paper›PMID 31062022›Full record

ArticleNucleic acids research2019

Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.

Ingrid Rössler, Julia Embacher, Benjamin Pillet, Guillaume Murat, Laura Liesinger, Jutta Hafner, Julia Judith Unterluggauer, Ruth Birner-Gruenberger, Dieter Kressler, Brigitte Pertschy

Open access · goldAbstract readComparative Study
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

31 citing papers in PubMed, 41 citations in OpenAlex.

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  8. Biallelic variants in the conserved ribosomal protein chaperone geneProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
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  12. Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024
    Review
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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 at 3 institutions in 2 countries.

Ingrid RösslerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Julia EmbacherInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Benjamin PilletUnit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.
Guillaume MuratUnit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.
Laura LiesingerBioTechMed-Graz, Graz, Austria.
Jutta HafnerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Julia Judith UnterluggauerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Ruth Birner-GruenbergerBioTechMed-Graz, Graz, Austria.
Dieter KresslerUnit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.
Brigitte PertschyInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
University of Graz · ATUniversity of Fribourg · CHMedical University of Graz · AT

Funding

Austrian Science Fund FWF KLI 425Austrian Science Fund FWF P 27996Austrian Science Fund FWF P 28874Austrian Science Fund FWF W 1226
6 · The paper itself

Abstract

Dedicated chaperones protect newly synthesized ribosomal proteins (r-proteins) from aggregation and accompany them on their way to assembly into nascent ribosomes. Currently, only nine of the ∼80 eukaryotic r-proteins are known to be guarded by such chaperones. In search of new dedicated r-protein chaperones, we performed a tandem-affinity purification based screen and looked for factors co-enriched with individual small subunit r-proteins. We report the identification of Nap1 and Tsr4 as direct binding partners of Rps6 and Rps2, respectively. Both factors promote the solubility of their r-protein clients in vitro. While Tsr4 is specific for Rps2, Nap1 has several interaction partners including Rps6 and two other r-proteins. Tsr4 binds co-translationally to the essential, eukaryote-specific N-terminal extension of Rps2, whereas Nap1 interacts with a large, mostly eukaryote-specific binding surface of Rps6. Mutation of the essential Tsr4 and deletion of the non-essential Nap1 both enhance the 40S synthesis defects of the corresponding r-protein mutants. Our findings highlight that the acquisition of eukaryote-specific domains in r-proteins was accompanied by the co-evolution of proteins specialized to protect these domains and emphasize the critical role of r-protein chaperones for the synthesis of eukaryotic ribosomes.

Indexed as

Amino Acid SequenceModels, MolecularMolecular ChaperonesNucleosome Assembly Protein 1Organelle BiogenesisProtein BindingProtein BiosynthesisProtein ConformationProtein DomainsProtein Interaction MappingRecombinant Fusion ProteinsRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentMolecular ChaperonesNAP1 protein, S cerevisiaeNucleosome Assembly Protein 1Recombinant Fusion ProteinsRibosomal ProteinsSaccharomyces cerevisiae ProteinsTSR4 protein, S cerevisiae

Identifiers

PMID31062022
PMCPMC6648895
OpenAlexW2944686971

What OpenQuestion holds

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LicenceCC BY
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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.