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Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs

Authors :
Danesh Moazed
André Verdel
Mohammad R. Motamedi
Steven P. Gygi
Scott A. Gerber
Serafin U. Colmenares
Verdel, Andre
Department of cell biology
Harvard Medical School
Taplin Biological Mass Spectrometry Facility
Source :
Cell, Cell, Elsevier, 2004, 119 (6), pp.789-802. <10.1016/j.cell.2004.11.034>
Publication Year :
2004

Abstract

International audience; RNAi-mediated heterochromatin assembly in fission yeast requires the RNA-induced transcriptional silencing (RITS) complex and a putative RNA-directed RNA polymerase (Rdp1). Here we show that Rdp1 is associated with two conserved proteins, Hrr1, an RNA helicase, and Cid12, a member of the polyA polymerase family, in a complex that has RNA-directed RNA polymerase activity (RDRC, RNA-directed RNA polymerase complex). RDRC physically interacts with RITS in a manner that requires the Dicer ribonuclease (Dcr1) and the Clr4 histone methyltransferase. Moreover, both complexes are localized to the nucleus and associate with noncoding centromeric RNAs in a Dcr1-dependent manner. In cells lacking Rdp1, Hrr1, or Cid12, RITS complexes are devoid of siRNAs and fail to localize to centromeric DNA repeats to initiate heterochromatin assembly. These findings reveal a physical and functional link between Rdp1 and RITS and suggest that noncoding RNAs provide a platform for siRNA-dependent localization of RNAi complexes to specific chromosome regions.

Details

ISSN :
00928674
Volume :
119
Issue :
6
Database :
OpenAIRE
Journal :
Cell
Accession number :
edsair.doi.dedup.....62e86a8ede4a4db40c71baed47c0a43e
Full Text :
https://doi.org/10.1016/j.cell.2004.11.034&gt;