Nucleosome-binding activities within JARID2 and EZH1 regulate the function of PRC2 on chromatin.
Nucleosome-binding activities within JARID2 and EZH1 regulate the function of PRC2 on chromatin.
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DOI：
10.1101/gad.225888.113
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发表时间：
2013-12-15
影响因子：
10.5
通讯作者：
Reinberg D
中科院分区：
文献类型：
--
作者：
Son J;Shen SS;Margueron R;Reinberg D
表观遗传调节剂Polycomb-repressive complex 2（PRC 2）通过其核心组分Ezh催化组蛋白3 Lys 27甲基化（H3 K27 me 3）。Reinberg及其同事研究了辅助因子Jarid 2和哺乳动物同系物Ezh 1/2如何影响PRC 2与核小体和染色质的结合。他们表明Jarid 2核小体结合活性有助于PRC 2刺激。有趣的是，与PRC 2-Ezh 2相反，PRC 2-Ezh 1表现出这种活性。这些数据表明了一个模型，其中PRC 2-Ezh 2对于在分裂细胞中建立H3 K27 me 3是重要的，而PRC 2-Ezh 1对于其在静息细胞中的维持是必需的。Polycomb-repressive complex 2（PRC 2）包含表观遗传调节剂Polycomb组的特定成员。PRC 2通过其zeste增强子（Ezh）组分催化组蛋白H3在Lys 27（H3 K27 me 3）的甲基化，其中有两种哺乳动物同源物：Ezh 1和Ezh 2。几个辅助因子，包括Jarid 2，调节PRC 2功能，Jarid 2促进其募集到靶基因。Jarid 2与Ezh 2一样，存在于分化不良和活跃分裂的细胞中，而Ezh 1在所有细胞中与PRC 2相关，包括静息细胞。我们发现Jarid 2表现出有助于PRC 2刺激的核小体结合活性。此外，与PRC 2-Ezh 2相反，包含Ezh 1的PRC 2（PRC 2-Ezh 1）表现出这种核小体结合活性。Ezh 1的存在有助于维持PRC 2在成肌细胞中对其靶基因的占据，其中Jarid 2不表达。我们的研究结果使我们能够提出一个模型，其中PRC 2-Ezh 2对于在分裂细胞中从头建立H3 K27 me 3是重要的，而PRC 2-Ezh 1是其在静息细胞中维持所必需的。
The epigenetic modulator Polycomb-repressive complex 2 (PRC2) catalyzes histone 3 Lys 27 methylation (H3K27me3) through its core component, Ezh. Here Reinberg and colleagues investigate how ancillary factor Jarid2 and mammalian homologs Ezh1/2 affect PRC2 engagement with nucleosomes and chromatin. They show that Jarid2 nucleosome-binding activity contributes to PRC2 stimulation. Interestingly, this activity is exhibited by PRC2–Ezh1, in contrast to PRC2–Ezh2. The data suggest a model in which PRC2–Ezh2 is important for establishing H3K27me3 in dividing cells, whereas PRC2–Ezh1 is required for its maintenance in resting cells. Polycomb-repressive complex 2 (PRC2) comprises specific members of the Polycomb group of epigenetic modulators. PRC2 catalyzes methylation of histone H3 at Lys 27 (H3K27me3) through its Enhancer of zeste (Ezh) constituent, of which there are two mammalian homologs: Ezh1 and Ezh2. Several ancillary factors, including Jarid2, modulate PRC2 function, with Jarid2 facilitating its recruitment to target genes. Jarid2, like Ezh2, is present in poorly differentiated and actively dividing cells, while Ezh1 associates with PRC2 in all cells, including resting cells. We found that Jarid2 exhibits nucleosome-binding activity that contributes to PRC2 stimulation. Moreover, such nucleosome-binding activity is exhibited by PRC2 comprising Ezh1 (PRC2–Ezh1), in contrast to PRC2–Ezh2. The presence of Ezh1 helps to maintain PRC2 occupancy on its target genes in myoblasts where Jarid2 is not expressed. Our findings allow us to propose a model in which PRC2–Ezh2 is important for the de novo establishment of H3K27me3 in dividing cells, whereas PRC2–Ezh1 is required for its maintenance in resting cells.
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