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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2007-2-19
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17189298-10202152,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17189298-9813005
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
789-800
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17189298-Cell Line, Tumor,
pubmed-meshheading:17189298-Cell Nucleolus,
pubmed-meshheading:17189298-Humans,
pubmed-meshheading:17189298-Nuclear Proteins,
pubmed-meshheading:17189298-Point Mutation,
pubmed-meshheading:17189298-Protein Structure, Tertiary,
pubmed-meshheading:17189298-Proteins,
pubmed-meshheading:17189298-RNA, Ribosomal,
pubmed-meshheading:17189298-RNA Interference,
pubmed-meshheading:17189298-RNA Processing, Post-Transcriptional,
pubmed-meshheading:17189298-Sequence Deletion
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pubmed:year |
2007
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pubmed:articleTitle |
The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing.
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pubmed:affiliation |
Institute of Clinical Molecular Biology and Tumour Genetics, GSF Research Centre, Marchioninistrasse 25, 81377 Munich, Germany. hoelzel@gsf.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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