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The Chp1-Tas3 core is a multifunctional platform critical for gene silencing by RITS.

Nat. Struct. Mol. Biol.2011 Nov 13;18(12):1351-7
Thomas Schalch 1 , Godwin Job , Sreenath Shanker , Janet F Partridge , Leemor Joshua-Tor
Thomas Schalch 1 , Godwin Job , Sreenath Shanker , Janet F Partridge , Leemor Joshua-Tor

[No authors listed]

Author information
  • 1 Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, USA.
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摘要


RNA interference is critical for the assembly of heterochromatin at Schizosaccharomyces pombe centromeres. Central to this process is the RNA-induced initiation of transcriptional gene silencing (RITS) complex, which physically anchors small noncoding RNAs to chromatin. RITS includes Ago1, the chromodomain protein Chp1, and Tas3, which forms a bridge between Chp1 and Ago1. Chp1 is a large protein with no recognizable domains, apart from its chromodomain. Here we describe how the structured C-terminal half of Chp1 binds the Tas3 N-terminal domain, revealing the tight association of Chp1 and Tas3. The structure also shows a PIN domain at the C-terminal tip of Chp1 that controls subtelomeric transcripts through a post-transcriptional mechanism. We suggest that the Chp1-Tas3 complex provides a solid and versatile platform to recruit both and gene-silencing pathways for locus-specific regulation of heterochromatin.