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


Journal

Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011

Informations de publication

Date de publication:
26 07 2019
Historique:
accepted: 19 04 2019
revised: 15 04 2019
received: 28 01 2019
pubmed: 8 5 2019
medline: 7 1 2020
entrez: 8 5 2019
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 31062022
pii: 5486275
doi: 10.1093/nar/gkz317
pmc: PMC6648895
doi:

Substances chimiques

Molecular Chaperones 0
NAP1 protein, S cerevisiae 0
Nucleosome Assembly Protein 1 0
Recombinant Fusion Proteins 0
Ribosomal Proteins 0
Saccharomyces cerevisiae Proteins 0
TSR4 protein, S cerevisiae 0

Types de publication

Comparative Study Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

6984-7002

Informations de copyright

© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.

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Auteurs

Ingrid Rössler (I)

Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
BioTechMed-Graz, Graz, Austria.

Julia Embacher (J)

Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
BioTechMed-Graz, Graz, Austria.

Benjamin Pillet (B)

Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.

Guillaume Murat (G)

Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.

Laura Liesinger (L)

BioTechMed-Graz, Graz, Austria.
Gottfried Schatz Research Center, Medical University of Graz, Graz, Austria.
Omics Center Graz, BioTechMed-Graz, Graz, Austria.

Jutta Hafner (J)

Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
BioTechMed-Graz, Graz, Austria.

Julia Judith Unterluggauer (JJ)

Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
BioTechMed-Graz, Graz, Austria.

Ruth Birner-Gruenberger (R)

BioTechMed-Graz, Graz, Austria.
Gottfried Schatz Research Center, Medical University of Graz, Graz, Austria.
Omics Center Graz, BioTechMed-Graz, Graz, Austria.

Dieter Kressler (D)

Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland.

Brigitte Pertschy (B)

Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria.
BioTechMed-Graz, Graz, Austria.

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Classifications MeSH