Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME
- Rössler, Ingrid Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria - BioTechMed-Graz, Graz, Austria
- Embacher, Julia Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria - BioTechMed-Graz, Graz, Austria
- Pillet, Benjamin Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland
- Murat, Guillaume Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland
- Liesinger, Laura BioTechMed-Graz, Graz, Austria - Gottfried Schatz Research Center, Medical University of Graz, Graz, Austria - Omics Center Graz, BioTechMed-Graz, Graz, Austria
- Hafner, Jutta Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria - BioTechMed-Graz, Graz, Austria
- Unterluggauer, Julia Judith Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria - BioTechMed-Graz, Graz, Austria
- Birner-Gruenberger, Ruth BioTechMed-Graz, Graz, Austria - Gottfried Schatz Research Center, Medical University of Graz, Graz, Austria - Omics Center Graz, BioTechMed-Graz, Graz, Austria
- Kressler, Dieter Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, 1700 Fribourg, Switzerland
- Pertschy, Brigitte Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, 8010 Graz, Austria - BioTechMed-Graz, Graz, Austria
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2019
Published in:
- Nucleic Acids Research. - 2019, p. gkz317
English
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.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 324635
- DOI 10.1093/nar/gkz317
- Persistent URL
- https://folia.unifr.ch/unifr/documents/307847
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