Saccharomyces cerevisiae nucleolar protein Nop7p is necessary for biogenesis of 60S ribosomal subunits
| Autor: | Judibelle Roman, Piyanun Harnpicharnchai, Cynthia C Adams, Jelena Jakovljevic, John L. Woolford |
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| Rok vydání: | 2002 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Genotype Nucleolus Recombinant Fusion Proteins Molecular Sequence Data 5.8S ribosomal RNA Ribosome biogenesis Saccharomyces cerevisiae Biology Ribosome Ribosome assembly Fungal Proteins Ribosomal protein Amino Acid Sequence Cloning Molecular Fluorescent Antibody Technique Indirect Molecular Biology Alleles DNA Primers Genetics Base Sequence Eukaryotic Large Ribosomal Subunit Nuclear Proteins Ribosomal RNA Recombinant Proteins Cell biology Mutagenesis Ribosomes Cell Nucleolus Research Article |
| Zdroj: | RNA. 8:150-165 |
| ISSN: | 1355-8382 |
| DOI: | 10.1017/s1355838202010026 |
| Popis: | To identify new gene products that participate in ribosome biogenesis, we carried out a screen for mutations that result in lethality in combination with mutations in DRS1, a Saccharomyces cerevisiae nucleolar DEAD-box protein required for synthesis of 60S ribosomal subunits. We identified the gene NOP7that encodes an essential protein. The temperature-sensitive nop7-1 mutation or metabolic depletion of Nop7p results in a deficiency of 60S ribosomal subunits and accumulation of halfmer polyribosomes. Analysis of pre-rRNA processing indicates that nop7 mutants exhibit a delay in processing of 27S pre-rRNA to mature 25S rRNA and decreased accumulation of 25S rRNA. Thus Nop7p, like Drs1p, is required for essential steps leading to synthesis of 60S ribosomal subunits. In addition, inactivation or depletion of Nop7p also affects processing at the A0, A1, and A2 sites, which may result from the association of Nop7p with 35S pre-rRNA in 90S pre-rRNPs. Nop7p is localized primarily in the nucleolus, where most steps in ribosome assembly occur. Nop7p is homologous to the zebrafish pescadillo protein necessary for embryonic development. The Nop7 protein contains the BRCT motif, a protein-protein interaction domain through which, for example, the human BRCA1 protein interacts with RNA helicase A. |
| Databáze: | OpenAIRE |
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