Department of Life Science, College of Natural Sciences, Research Center for Biomolecules and Biosystems, Chung-Ang University, Seoul 156-756, Republic of Korea.
FEBS Lett. 2012 Sep 21;586(19):3159-65. doi: 10.1016/j.febslet.2012.06.026. Epub 2012 Jul 13.
Significant progress has been made in understanding the relationship between histone modifications and 'reader' molecules and their effects on transcriptional regulation. A previously identified INHAT complex subunit, SET/TAF-Iβ, binds to histones and inhibits histone acetylation. To investigate the binding specificities of SET/TAF-Iβ to various histone modifications, we employed modified histone tail peptide array analyses. SET/TAF-Iβ strongly recognized PRC2-mediated H3K27me1/2/3; however, the bindings were completely disrupted by H3S28 phosphorylation. We have demonstrated that SET/TAF-Iβ is sequentially recruited to the target gene promoter ATF3 after the PRC2 complex via H3K27me recognition and may offer additive effects in the repression of the target gene.
在理解组蛋白修饰与“读取器”分子之间的关系及其对转录调控的影响方面已经取得了重大进展。先前鉴定的 INHAT 复合物亚基 SET/TAF-Iβ 与组蛋白结合并抑制组蛋白乙酰化。为了研究 SET/TAF-Iβ 与各种组蛋白修饰的结合特异性，我们采用了修饰组蛋白尾部肽阵列分析。SET/TAF-Iβ 强烈识别 PRC2 介导的 H3K27me1/2/3；然而，H3S28 磷酸化完全破坏了结合。我们已经证明，SET/TAF-Iβ 通过 H3K27me 识别后，在 PRC2 复合物之后被顺序招募到靶基因启动子 ATF3，并且在靶基因的抑制中可能具有附加效应。
