Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement.
Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement.
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DOI：
10.1016/j.cell.2013.08.005
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发表时间：
2013-09-12
期刊：
影响因子：
64.5
通讯作者：
Wu C
中科院分区：
文献类型：
--
作者：
Ranjan A;Mizuguchi G;FitzGerald PC;Wei D;Wang F;Huang Y;Luk E;Woodcock CL;Wu C
组蛋白变异体H_2A.Z是真核生物调控DNA近端的核小体的全基因组标记。虽然已知多亚基染色质重构体SWR1催化依赖于ATP的H2A.Z沉积，但SWR1募集到酿酒酵母启动子的机制尚不清楚。对双核小体底物竞争结合的灵敏分析表明，SWR1优先结合长的无核小体DNA和相邻的核小体核心颗粒，允许基因启动子相对于基因体的区分。对突变体的分析表明，Swr1保守的Swc2/YL1亚基和ATPase结构域主要负责与底物结合。在由NuA4组蛋白乙酰转移酶乙酰化的核小体上，SWR1的结合增强，但对无核小体和核小体DNA的识别主导于与乙酰化组蛋白的相互作用。DNA和组蛋白信号之间的这种分层合作扩大了遗传开关的动态范围，将DNA结合因子对经典基因的调控与ATP依赖的核小体重塑和翻译后组蛋白修饰统一起来。
The histone variant H2A.Z is a genome-wide signature of nucleosomes proximal to eukaryotic regulatory DNA. While the multi-subunit chromatin remodeler SWR1 is known to catalyze ATP-dependent deposition of H2A.Z, the mechanism of SWR1 recruitment to S. cerevisiae promoters has been unclear. A sensitive assay for competitive binding of di-nucleosome substrates revealed that SWR1 preferentially binds long nucleosome-free DNA and the adjoining nucleosome core particle, allowing discrimination of gene promoters over gene bodies. Analysis of mutants indicates that the conserved Swc2/YL1 subunit and the ATPase domain of Swr1 are mainly responsible for binding to substrate. SWR1 binding is enhanced on nucleosomes acetylated by the NuA4 histone acetyltransferase, but recognition of nucleosome-free and nucleosomal DNA is dominant over interaction with acetylated histones. Such hierarchical cooperation between DNA and histone signals expands the dynamic range of genetic switches, unifying classical gene regulation by DNA-binding factors with ATP-dependent nucleosome remodeling and post-translational histone modifications.
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