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

Nucleic Acids Res. 35, 789-800 (2007)
Verlagsversion Volltext DOI
Open Access Gold
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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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter FACTOR TIF-IA; CELL-PROLIFERATION; PROTEIN L11; DNA-DAMAGE; BIOGENESIS; CYCLE; P53; PESCADILLO; COMPLEX; STRESS
ISSN (print) / ISBN 0305-1048
e-ISSN 1362-4962
Quellenangaben Band: 35, Heft: 3, Seiten: 789-800 Artikelnummer: , Supplement: ,
Verlag Oxford University Press
Begutachtungsstatus