The Essential Nucleolar Yeast Protein Nop8p Controls the Exosome Function during 60S Ribosomal Subunit Maturation
| Autor: | Carla C. Oliveira, Mauricio B. Goldfeder, Nilson Ivo Tonin Zanchin, Marcia Cristina Teixeira Dos Santos |
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| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Nucleolus Protein subunit Saccharomyces cerevisiae lcsh:Medicine Biology Exosomes Ribosome Biochemistry Ribonucleases Genetics lcsh:Science Protein Interactions Multidisciplinary Eukaryotic Large Ribosomal Subunit lcsh:R Proteins Ribosomal RNA Ribosome Subunits Large Eukaryotic biology.organism_classification Molecular biology Cell biology RNA Ribosomal 5.8S Nucleic acids RNA processing Ribosome Subunits TRAMP complex Trans-Activators BIOQUÍMICA RNA lcsh:Q Cell Nucleolus Research Article |
| Zdroj: | PLoS ONE Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP PLoS ONE, Vol 6, Iss 6, p e21686 (2011) |
| ISSN: | 1932-6203 |
| Popis: | The yeast nucleolar protein Nop8p has previously been shown to interact with Nip7p and to be required for 60S ribosomal subunit formation. Although depletion of Nop8p in yeast cells leads to premature degradation of rRNAs, the biochemical mechanism responsible for this phenotype is still not known. In this work, we show that the Nop8p amino-terminal region mediates interaction with the 5.8S rRNA, while its carboxyl-terminal portion interacts with Nip7p and can partially complement the growth defect of the conditional mutant strain Δnop8/GAL::NOP8. Interestingly, Nop8p mediates association of Nip7p to pre-ribosomal particles. Nop8p also interacts with the exosome subunit Rrp6p and inhibits the complex activity in vitro, suggesting that the decrease in 60S ribosomal subunit levels detected upon depletion of Nop8p may result from degradation of pre-rRNAs by the exosome. These results strongly indicate that Nop8p may control the exosome function during pre-rRNA processing. |
| Databáze: | OpenAIRE |
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