Journal
MOLECULAR CELL
Volume 34, Issue 1, Pages 36-46Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2009.02.024
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Funding
- NIH [1R01-GM084045, GM072659]
- Cancer Center support [CCSG 2 P30 CA 21765-25, -26, CA21765]
- American Lebanese Syrian Associated Charities
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In fission yeast, assembly of centromeric heterochromatin requires the RITS complex, which consists of Ago1, Tas3, Chp1, and siRNAs derived from centromeric repeats. Recruitment of RITS to centromeres has been proposed to depend on siRNA-dependent targeting of Ago1 to centromeric sequences. Previously, we demonstrated that methylated lysine 9 of histone H3 (H3K9me) acts upstream of siRNAs during heterochromatin establishment. Our crystal structure of Chp1's chromodomain in complex with a trimethylated lysine 9 H3 peptide reveals extensive sites of contact that contribute to Chp1's high-affinity binding. We found that this high-affinity binding is critical for the efficient establishment of centromeric heterochromatin, but preassembled heterochromatin can be maintained when Chp1's affinity for H3K9me is greatly reduced.
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