Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI
Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI
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DOI：
10.1016/s1097-2765(03)00273-9
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发表时间：
2003-08-01
期刊：
影响因子：
16
通讯作者：
Müller, CW
中科院分区：
文献类型：
--
作者：
Grüne, T;Brzeski, J;Müller, CW
能量依赖的核小体重塑是赋予染色质动力学性质的关键过程。然而，重塑ATP酶与其核小体底物相互作用以改变组蛋白-DNA相互作用的原理知之甚少。我们已经确定了一个底物识别结构域的C-末端的一半重塑ATP酶ISWI和确定其结构的X-射线晶体学。该结构包括三个结构域，一个具有新折叠的四螺旋结构域和两个与c-Myb、SANT和SLIDE模块相关的α-螺旋结构域，它们通过沿着螺旋连接。这些结构域的综合结构和功能分析提供了深入了解ISWI如何与核小体底物相互作用。
Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two a-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by along helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate.