ATP-dependent histone octamer mobilization and histone deacetylation mediated by the Mi-2 chromatin remodeling complex
ATP-dependent histone octamer mobilization and histone deacetylation mediated by the Mi-2 chromatin remodeling complex
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DOI：
10.1021/bi000421t
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发表时间：
2000-05-09
期刊：
影响因子：
2.9
通讯作者：
Wolffe, AP
中科院分区：
文献类型：
--
作者：
Guschin, D;Wade, PA;Wolffe, AP
Mi-2复合物与组蛋白脱乙酰化相关的染色质重塑和转录抑制有关。在这里，我们使用一个纯化的Mi-2复合物含有六个组件，Mi-2，Mta 1样，p66，RbAp 48，RPD 3，和MBD 3，研究这种复合物的能力，使组蛋白-DNA相互作用不稳定和去乙酰化核心组蛋白。Mi-2复合物具有ATP酶活性，该活性受核小体刺激，但不受游离组蛋白或DNA刺激。这种核小体ATP酶相对低效，但对于促进组蛋白八聚体相对于DNA的翻译运动和单核小体内核心组蛋白的有效脱乙酰化是必不可少的。令人惊讶的是，ATP酶活性对核小体阵列的脱乙酰化没有影响。
The Mi-2 complex has been implicated in chromatin remodeling and transcriptional repression associated with histone deacetylation. Here, we use a purified Mi-2 complex containing six components, Mi-2, Mta 1-like, p66, RbAp48, RPD3, and MBD3, to investigate the capacity of this complex to destabilize histone-DNA interactions and deacetylate core histones. The Mi-2 complex has ATPase activity that is stimulated by nucleosomes but not by free histones or DNA. This nucleosomal ATPase is relatively inefficient, yet is essential to facilitate both translational movement of histone octamers relative to DNA and the efficient deacetylation of the core histones within a mononucleosome. Surprisingly, ATPase activity had no effect on deacetylation of nucleosomal arrays.