Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
复制标题
DOI：
10.1074/jbc.c200045200
复制
发表时间：
2002-04-05
影响因子：
4.8
通讯作者：
Kouzarides, T
中科院分区：
文献类型：
--
作者：
Zegerman, P;Canas, B;Kouzarides, T
组蛋白 N 末端尾部以多种方式进行翻译后修饰。在赖氨酸残基处，组蛋白可以被乙酰化或甲基化。这两种修饰都会导致特定蛋白质的结合；溴结构域蛋白（例如 GCN5）结合乙酰赖氨酸，而染色结构域蛋白 HP1 结合组蛋白 H3 的甲基赖氨酸 9。在这里，我们展示了先前表征的转录阻遏复合物 NuRD（核小体重塑和脱乙酰酶）与组蛋白 H3 N 末端尾部结合，并且赖氨酸 4（而非赖氨酸 9）的甲基化阻止了结合。鉴于赖氨酸 4 甲基化存在于活性转录位点，这些结果表明赖氨酸 4 甲基化的功能是破坏组蛋白与阻遏物复合物的关联。
Histone N-terminal tails are post-translationally modified in many ways. At lysine residues, histones can be either acetylated or methylated. Both modifications lead to the binding of specific proteins; bromodomain proteins, such as GCN5, bind acetyl lysines and the chromodomain protein, HP1, binds methyl lysine 9 of histone H3. Here we show that the previously characterized transcriptional repressor complex NuRD (nucleosome remodeling and deacetylase) binds to the histone H3 N-terminal tail and that methylation at lysine 4, but not lysine 9, prevents binding. Given that lysine 4 methylation is found at sites of active transcription, these results suggest that a function of lysine 4 methylation is to disrupt the association of histones with a repressor complex.