组蛋白H3
组蛋白甲基转移酶
组蛋白密码
组蛋白
生物
组蛋白甲基化
组蛋白H2A
异染色质蛋白1
染色质
异染色质
化学
细胞生物学
核小体
EZH2型
遗传学
DNA甲基化
基因表达
基因
作者
Monika Lachner,Dónal O’Carroll,Stephen Rea,Karl Mechtler,Thomas Jenuwein
出处
期刊:Nature
[Springer Nature]
日期:2001-03-01
卷期号:410 (6824): 116-120
被引量:2721
摘要
Distinct modifications of histone amino termini, such as acetylation, phosphorylation and methylation, have been proposed to underlie a chromatin-based regulatory mechanism that modulates the accessibility of genetic information. In addition to histone modifications that facilitate gene activity, it is of similar importance to restrict inappropriate gene expression if cellular and developmental programmes are to proceed unperturbed. Here we show that mammalian methyltransferases that selectively methylate histone H3 on lysine 9 (Suv39h HMTases) generate a binding site for HP1 proteins--a family of heterochromatic adaptor molecules implicated in both gene silencing and supra-nucleosomal chromatin structure. High-affinity in vitro recognition of a methylated histone H3 peptide by HP1 requires a functional chromo domain; thus, the HP1 chromo domain is a specific interaction motif for the methyl epitope on lysine9 of histone H3. In vivo, heterochromatin association of HP1 proteins is lost in Suv39h double-null primary mouse fibroblasts but is restored after the re-introduction of a catalytically active SWUV39H1 HMTase. Our data define a molecular mechanism through which the SUV39H-HP1 methylation system can contribute to the propagation of heterochromatic subdomains in native chromatin.
科研通智能强力驱动
Strongly Powered by AbleSci AI