| pubmed-article:17189298 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17189298 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:17189298 | lifeskim:mentions | umls-concept:C1418467 | lld:lifeskim |
| pubmed-article:17189298 | lifeskim:mentions | umls-concept:C1511026 | lld:lifeskim |
| pubmed-article:17189298 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:17189298 | lifeskim:mentions | umls-concept:C1156152 | lld:lifeskim |
| pubmed-article:17189298 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:17189298 | pubmed:dateCreated | 2007-2-19 | lld:pubmed |
| pubmed-article:17189298 | 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. | lld:pubmed |
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| pubmed-article:17189298 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17189298 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17189298 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17189298 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17189298 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:17189298 | pubmed:author | pubmed-author:YunN RNR | lld:pubmed |
| pubmed-article:17189298 | pubmed:author | pubmed-author:KremmerElisab... | lld:pubmed |
| pubmed-article:17189298 | pubmed:author | pubmed-author:GrimmThomasT | lld:pubmed |
| pubmed-article:17189298 | pubmed:author | pubmed-author:HölzelMichael... | lld:pubmed |
| pubmed-article:17189298 | pubmed:author | pubmed-author:RohrmoserMich... | lld:pubmed |
| pubmed-article:17189298 | pubmed:author | pubmed-author:HarasimThomas... | lld:pubmed |
| pubmed-article:17189298 | pubmed:author | pubmed-author:MalamoussiAna... | lld:pubmed |
| pubmed-article:17189298 | pubmed:author | pubmed-author:Gruber-EberAn... | lld:pubmed |
| pubmed-article:17189298 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17189298 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:17189298 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17189298 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17189298 | pubmed:pagination | 789-800 | lld:pubmed |
| pubmed-article:17189298 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17189298 | pubmed:meshHeading | pubmed-meshheading:17189298... | lld:pubmed |
| pubmed-article:17189298 | pubmed:meshHeading | pubmed-meshheading:17189298... | lld:pubmed |
| pubmed-article:17189298 | pubmed:meshHeading | pubmed-meshheading:17189298... | lld:pubmed |
| pubmed-article:17189298 | pubmed:meshHeading | pubmed-meshheading:17189298... | lld:pubmed |
| pubmed-article:17189298 | pubmed:meshHeading | pubmed-meshheading:17189298... | lld:pubmed |
| pubmed-article:17189298 | pubmed:meshHeading | pubmed-meshheading:17189298... | lld:pubmed |
| pubmed-article:17189298 | pubmed:meshHeading | pubmed-meshheading:17189298... | lld:pubmed |
| pubmed-article:17189298 | pubmed:meshHeading | pubmed-meshheading:17189298... | lld:pubmed |
| pubmed-article:17189298 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17189298 | pubmed:articleTitle | The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing. | lld:pubmed |
| pubmed-article:17189298 | pubmed:affiliation | Institute of Clinical Molecular Biology and Tumour Genetics, GSF Research Centre, Marchioninistrasse 25, 81377 Munich, Germany. hoelzel@gsf.de | lld:pubmed |
| pubmed-article:17189298 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17189298 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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