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Nucleic Acids Research Advance Access published online on December 22, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl1058
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© 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.

RNA

The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing

Michael Hölzel*, Thomas Grimm, Michaela Rohrmoser, Anastassia Malamoussi, Thomas Harasim, Anita Gruber-Eber, Elisabeth Kremmer1 and Dirk Eick*

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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M. Rohrmoser, M. Holzel, T. Grimm, A. Malamoussi, T. Harasim, M. Orban, I. Pfisterer, A. Gruber-Eber, E. Kremmer, and D. Eick
Interdependence of Pes1, Bop1, and WDR12 Controls Nucleolar Localization and Assembly of the PeBoW Complex Required for Maturation of the 60S Ribosomal Subunit
Mol. Cell. Biol., May 15, 2007; 27(10): 3682 - 3694.
[Abstract] [Full Text] [PDF]


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