DEAD-box helicase DDX27 regulates 3' end formation of ribosomal 47S RNA and stably associates with the PeBoW-complex

Autor:	Michaela Rohrmoser, Axel Imhof, Kirsten Voss, Kaspar Burger, Elisabeth Kremmer, Bastian Mühl, Anita Gruber-Eber, Markus Kellner, Ignasi Forné, Dirk Eick
Rok vydání:	2014
Předmět:	Nucleolus Helicase RNA Nuclear Proteins Proteins RNA-Binding Proteins Cell Cycle Proteins Cell Biology Ribosomal RNA Biology RNA Helicase A Molecular biology PeBoW complex DEAD-box RNA Helicases BOP1 RNA Ribosomal Multiprotein Complexes biology.protein Tumor Cells Cultured Humans RRNA processing
Zdroj:	Experimental cell research. 334(1)
ISSN:	1090-2422
Popis:	PeBoW, a trimeric complex consisting of pescadillo (Pes1), block of proliferation (Bop1), and the WD repeat protein 12 (WDR12), is essential for processing and maturation of mammalian 5.8S and 28S ribosomal RNAs. Applying a mass spectrometric analysis, we identified the DEAD-box helicase DDX27 as stably associated factor of the PeBoW-complex. DDX27 interacts with the PeBoW-complex via an evolutionary conserved F×F motif in the N-terminal domain and is recruited to the nucleolus via its basic C-terminal domain. This recruitment is RNA-dependent and occurs independently of the PeBoW-complex. Interestingly, knockdown of DDX27, but not of Pes1, induces the accumulation of an extended form of the primary 47S rRNA. We conclude that DDX27 can interact specifically with the Pes1 and Bop1 but fulfils critical function(s) for proper 3′ end formation of 47S rRNA independently of the PeBoW-complex.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b664b4d7a296adb5095a8dad0881fec https://pubmed.ncbi.nlm.nih.gov/25825154 Zobrazit plný text záznamu Full Text from ScienceDirect