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Coordinated regulation of active and repressive histone methylations by a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans

热1 yonghao616 添加于 2010-6-26 19:32 | 2618 次阅读 | 1 个评论

作者
Lin H, Wang Y, Wang Y, Tian F, Pu P, Yu Y, Mao H, Yang Y, Wang P, Hu L, Lin Y, Liu Y, Xu Y, Chen CD
摘要
H3K9me2 and H3K27me2 are important epigenetic marks associated with transcription repression, while H3K4me3 is associated with transcription activation. It has been shown that active and repressive histone methylations distribute in a mutually exclusive manner, but the underlying mechanism was poorly understood. Here we identified ceKDM7A, a PHD (plant homeodomain)- and JmjC domain-containing protein, as a histone demethylase specific for H3K9me2 and H3K27me2. We further demonstrated that the PHD domain of ceKDM7A bound H3K4me3 and H3K4me3 co-localized with ceKDM7A at the genome-wide level. Disruption of the PHD domain binding to H3K4me3 reduced the demethylase activity in vivo, and loss of ceKDM7A reduced the expression of its associated target genes. These results indicate that ceKDM7A is recruited to the promoter to demethylate H3K9me2 and H3K27me2 and activate gene expression through the binding of the PHD domain to H3K4me3. Thus, our study identifies a dual-specificity histone demethylase and provides novel insights into the regulation of histone methylation.
详细资料
- 文献种类:期刊
- 期刊名称: Cell Research
- 期刊缩写: Cell Res
- 期卷页: 2010年
- ISBN: 1001-0602
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一个组蛋白去甲基化酶的特定作用方式

我们知道像H3K9me2和H3K27me2是和基因转录抑制相关的表观标记，而H3K4me3正好相反，是和基因的转录激活相关的。两者的分布应该是相互排斥的。对一个组蛋白去甲基化酶ceKDM7A的研究发现，它不但含有JmjC结构域，还含有一个PHD（plant homeodomain）结构域。研究发现PHD域可以识别H3K4me3，即该组蛋白去甲基化酶识别某基因启动子区域的H3k4me3，然后行使去甲基化功能，去除该基因区域的H3K9me2和H3K27me2，进而激活该基因的表达。

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