The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing
| Autor: | Anastassia Malamoussi, Elisabeth Kremmer, Anita Gruber-Eber, Michael Hölzel, Thomas Harasim, Michaela Rohrmoser, Dirk Eick, Thomas Grimm |
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| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Genetics
Nucleolus Point mutation Nuclear Proteins Proteins RNA-Binding Proteins Ribosomal RNA Biology Ribosome Cell biology Protein Structure Tertiary BRCT domain BOP1 RNA Ribosomal Cell Line Tumor Humans Point Mutation RNA RNA Interference Nuclear protein RNA Processing Post-Transcriptional RRNA processing Cell Nucleolus Sequence Deletion |
| Zdroj: | Nucleic Acids Res. 35, 789-800 (2007) Nucleic Acids Research |
| Popis: | The nucleolar protein Pes1 interacts with Bop1 and WDR12 in a stable complex (PeBoW-complex) and its expression is tightly associated with cell proliferation. The yeast homologue Nop7p (Yph1p) functions in both, rRNA processing and cell cycle progression. The presence of a BRCT-domain (BRCA1 C-terminal) within Pes1 is quite unique for an rRNA processing factor, as this domain is normally found in factors involved in DNA-damage or repair pathways. Thus, the function of the BRCT-domain in Pes1 remains elusive. We established a conditional siRNA-based knock-down-knock-in system and analysed a panel of Pes1 truncation mutants for their functionality in ribosome synthesis in the absence of endogenous Pes1. Deletion of the BRCT-domain or single point mutations of highly conserved residues caused diffuse nucleoplasmic distribution and failure to replace endogenous Pes1 in rRNA processing. Further, the BRCT-mutants of Pes1 were less stable and not incorporated into the PeBoW-complex. Hence, the integrity of the BRCT-domain of Pes1 is crucial for nucleolar localization and its function in rRNA processing. |
| Databáze: | OpenAIRE |
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