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首页> 外文期刊>Genes and Development: a Journal Devoted to the Molecular Analysis of Gene Expression in Eukaryotes, Prokaryotes, and Viruses >Diverse ways to be specific: a novel Zn-binding domain confers substrate specificity to UTX/KDM6A histone H3 Lys 27 demethylase.
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Diverse ways to be specific: a novel Zn-binding domain confers substrate specificity to UTX/KDM6A histone H3 Lys 27 demethylase.

机译:具体方法多样:一种新型的Zn结合结构域赋予UTX / KDM6A组蛋白H3 Lys 27脱甲基酶底物特异性。

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摘要

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.
机译:组蛋白甲基化受到位点特异性组蛋白甲基转移酶和脱甲基酶的高度调控。在本期《基因与发展》中,Sengoku和Yokoyama(pp。2266-2277)证明了UTX / KDM6A的新型Zn结合结构域和Jumonji结构域(Lys脱甲基酶6A)识别组蛋白H3,并一起作为底物特异性的决定因素用于H3K27脱甲基。这项研究证明了UTX / KDM6A进行位点特异性脱甲基的机制,并暗示组蛋白脱甲基酶使用多种方法来实现靶标特异性。

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