Centromeric heterochromatin assembly in fission yeast requires the RNAi pathway. 
Chp1, a chromodomain (CD) protein, forms the Ago1-containing RNA-induced 
transcriptional silencing (RITS) complex and recruits siRNA-bound RITS to 
methylated histone H3 lysine 9 (H3K9me) via its CD. Here, we show that the CD of 
Chp1 (Chp1-CD) possesses unique nucleic acid-binding activities that are 
essential for heterochromatic gene silencing. Detailed electrophoretic-mobility 
shift analyses demonstrated that Chp1 binds to RNA via the CD in addition to its 
central RNA-recognition motif. Interestingly, robust RNA- and DNA-binding 
activity of Chp1-CD was strongly enhanced when it was bound to H3K9me, which was 
revealed to involve a positively charged domain within the Chp1-CD by structural 
analyses. These results demonstrate a role for the CD that provides a link 
between RNA, DNA, and methylated histone tails to ensure heterochromatic gene 
silencing.