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http://purl.uniprot.org/citations/17189298http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17189298http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17189298http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkl1058"xsd:string
http://purl.uniprot.org/citations/17189298http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkl1058"xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Kremmer E."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Kremmer E."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Grimm T."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Grimm T."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Eick D."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Eick D."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Gruber-Eber A."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Gruber-Eber A."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Harasim T."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Harasim T."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Hoelzel M."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Hoelzel M."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Malamoussi A."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Malamoussi A."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Rohrmoser M."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/author"Rohrmoser M."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/17189298http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string