High-Affinity Binding of Chp1 Chromodomain to K9 Methylated Histone H3 Is Required to Establish Centromeric Heterochromatin

被引：102

作者：

Schalch, Thomas ^{[1
]}

Job, Godwin ^{[2
]}

Noffsinger, Victoria J. ^{[2
]}

Shanker, Sreenath ^{[2
]}

Kuscu, Canan ^{[1
,3
]}

Joshua-Tor, Leemor ^{[1
]}

Partridge, Janet F. ^{[2
]}

机构：

[1] Cold Spring Harbor Lab, Howard Hughes Med Inst, Keck Struct Biol Lab, Cold Spring Harbor, NY 11724 USA

[2] St Jude Childrens Res Hosp, Dept Biochem, Memphis, TN 38105 USA

[3] SUNY Stony Brook, Grad Program Biochem & Struct Biol, Stony Brook, NY 11794 USA

来源：

MOLECULAR CELL | 2009年 / 34卷 / 01期

关键词：

FISSION YEAST CENTROMERES; LYSINE-9; METHYLATION; EPIGENETIC CONTROL; HP1; PROTEIN; RNAI; DOMAIN; MAINTENANCE; RITS; COMPLEXES;

D O I：

10.1016/j.molcel.2009.02.024

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：36 / 46

页数：11

共 24 条

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