The eukaryote-specific N-terminal extension of ribosomal protein S31 contributes to the assembly and function of 40S ribosomal subunits
| Autor: | Guillaume Murat, Dieter Kressler, Antonio Fernández-Pevida, Sara Martín-Villanueva, Jesús de la Cruz, Thierry Lacombe |
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| Přispěvatelé: | Universidad de Sevilla. Departamento de Genética, Ministerio de Economía y Competitividad (MINECO). España |
| Rok vydání: | 2016 |
| Předmět: |
Ribosomal Proteins
0301 basic medicine Saccharomyces cerevisiae Proteins Protein subunit Nuclear Localization Signals Ribosome biogenesis Saccharomyces cerevisiae Biology Ribosome 03 medical and health sciences Ribosomal protein Genetics Eukaryotic Small Ribosomal Subunit RNA Processing Post-Transcriptional Molecular Biology Alleles Ribosome Subunits Small Eukaryotic Molecular biology Anti-Bacterial Agents Cell biology Aminoglycosides Phenotype 030104 developmental biology Ribosome Subunits Polyribosomes Protein Biosynthesis Mutation Nuclear transport Cell Nucleolus Nuclear localization sequence |
| Zdroj: | NUCLEIC ACIDS RESEARCH Nucleic Acids Research idUS. Depósito de Investigación de la Universidad de Sevilla instname |
| Popis: | The archaea-/eukaryote-specific 40S-ribosomal-subunit protein S31 is expressed as an ubiquitin fusion protein in eukaryotes and consists of a conserved body and a eukaryote-specific N-terminal extension. In yeast, S31 is a practically essential protein, which is required for cytoplasmic 20S pre-rRNA maturation. Here, we have studied the role of the N-terminal extension of the yeast S31 protein. We show that deletion of this extension partially impairs cell growth and 40S subunit biogenesis and confers hypersensitivity to aminoglycoside antibiotics. Moreover, the extension harbours a nuclear localization signal that promotes active nuclear import of S31, which associates with pre-ribosomal particles in the nucleus. In the absence of the extension, truncated S31 inefficiently assembles into pre-40S particles and two subpopulations of mature small subunits, one lacking and another one containing truncated S31, can be identified. Plasmid-driven overexpression of truncated S31 partially suppresses the growth and ribosome biogenesis defects but, conversely, slightly enhances the hypersensitivity to aminoglycosides. Altogether, these results indicate that the N-terminal extension facilitates the assembly of S31 into pre-40S particles and contributes to the optimal translational activity of mature 40S subunits but has only a minor role in cytoplasmic cleavage of 20S pre-rRNA at site D Ministerio de Economía y Competitividad BFU2013-42958-P |
| Databáze: | OpenAIRE |
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