Nucleic Acids Research Advance Access originally published online on December 22, 2006
Nucleic Acids Research 2007 35(3):789-800; doi:10.1093/nar/gkl1058
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Nucleic Acids Research, 2007, Vol. 35, No. 3 789-800
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing
Institute of Clinical Molecular Biology and Tumour Genetics, GSF Research Centre Marchioninistrasse 25, 81377 Munich, Germany 1 Institute of Molecular Immunology, GSF Research Centre Marchioninistrasse 25, 81377 Munich, Germany
*To whom correspondence should be addressed. Tel: +49897099512; Fax: +49897099500; Email: hoelzel{at}gsf.de
*Correspondence may also be addressed to Dirk Eick. Tel: +49897099512; Fax: +49897099500; Email: eick{at}gsf.de
Received July 14, 2006. Revised November 7, 2006. Accepted November 7, 2006.
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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