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

Exp Cell Res. 2015 May 15;334(1):146-59. doi: 10.1016/j.yexcr.2015.03.017. Epub 2015 Mar 28.

Abstract

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.

Keywords: DEAD-box helicase; F×F motif; Nucleolus; PeBoW-complex; rRNA processing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins
  • DEAD-box RNA Helicases / metabolism*
  • Humans
  • Multiprotein Complexes / metabolism
  • Nuclear Proteins / metabolism*
  • Proteins / metabolism*
  • RNA, Ribosomal / metabolism*
  • RNA-Binding Proteins
  • Tumor Cells, Cultured

Substances

  • BOP1 protein, human
  • Cell Cycle Proteins
  • Multiprotein Complexes
  • Nuclear Proteins
  • PES1 protein, human
  • Proteins
  • RNA, Ribosomal
  • RNA-Binding Proteins
  • WDR12 protein, human
  • DDX27 protein, human
  • DEAD-box RNA Helicases