Structural Genomics Consortium, University of Toronto, 101 College St., Toronto, Ontario M5G 1L7, Canada.
Biochem Biophys Res Commun. 2013 Jan 11;430(2):547-53. doi: 10.1016/j.bbrc.2012.11.116. Epub 2012 Dec 7.
PRC2 is the major H3K27 methyltransferase and is responsible for maintaining repressed gene expression patterns throughout development. It contains four core components: EZH2, EED, SUZ12 and RbAp46/48 and some cell-type specific components. In this study, we focused on characterizing the histone binding domains of PHF1 and PHF19, and found that the Tudor domains of PHF1 and PHF19 selectively bind to histone H3K36me3. Structural analysis of these Tudor domains also shed light on how these Tudor domains selectively bind to histone H3K36me3. The histone H3K36me3 binding by the Tudor domains of PHF1, PHF19 and likely MTF2 provide another recruitment and regulatory mechanism for the PRC2 complex. In addition, we found that the first PHD domains of PHF1 and PHF19 do not exhibit histone H3K4 binding ability, nor do they affect the Tudor domain binding to histones.
PRC2 是主要的 H3K27 甲基转移酶,负责在整个发育过程中维持被抑制的基因表达模式。它包含四个核心组件:EZH2、EED、SUZ12 和 RbAp46/48,以及一些细胞类型特异性组件。在这项研究中,我们专注于表征 PHF1 和 PHF19 的组蛋白结合结构域,发现 PHF1 和 PHF19 的 Tudor 结构域选择性地结合组蛋白 H3K36me3。这些 Tudor 结构域的结构分析也揭示了这些 Tudor 结构域如何选择性地结合组蛋白 H3K36me3。PHF1、PHF19 和可能的 MTF2 的 Tudor 结构域与组蛋白 H3K36me3 的结合为 PRC2 复合物提供了另一种募集和调节机制。此外,我们发现 PHF1 和 PHF19 的第一个 PHD 结构域不具有组蛋白 H3K4 结合能力,也不影响 Tudor 结构域与组蛋白的结合。