Department of Biological Sciences, Graduate School of Nanoscience and Technology (WCU), KAIST, Daejeon, South Korea.
Genes Dev. 2011 Nov 1;25(21):2223-6. doi: 10.1101/gad.179473.111.
Histone methylations are highly regulated by site-specific histone methyltransferases and demethylases. In this issue of Genes & Development, Sengoku and Yokoyama (pp. 2266-2277) demonstrate that a novel Zn-binding domain and the Jumonji domain of UTX/KDM6A (Lys demethylase 6A) recognize histone H3 and together function as a substrate specificity determinant for H3K27 demethylation. This study demonstrates the mechanism of site-specific demethylation by UTX/KDM6A and implicates that histone demethylases use diverse methods to accomplish target specificity.
组蛋白甲基化受到特定的组蛋白甲基转移酶和去甲基酶的高度调控。在本期《基因与发育》中,Sengoku 和 Yokoyama(第 2266-2277 页)证明了一个新的 Zn 结合域和 UTX/KDM6A(赖氨酸去甲基酶 6A)的 Jumonji 结构域识别组蛋白 H3,并共同作为 H3K27 去甲基化的底物特异性决定因素发挥作用。这项研究证明了 UTX/KDM6A 的位点特异性去甲基化机制,并暗示组蛋白去甲基酶使用多种方法来实现靶标特异性。