Structure of Actin-related protein 8 and its contribution to nucleosome binding.
Structure of Actin-related protein 8 and its contribution to nucleosome binding.
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DOI：
10.1093/nar/gks842
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发表时间：
2012-11
影响因子：
14.9
通讯作者：
Hopfner KP
中科院分区：
文献类型：
--
作者：
Gerhold CB;Winkler DD;Lakomek K;Seifert FU;Fenn S;Kessler B;Witte G;Luger K;Hopfner KP
核肌动蛋白相关蛋白(ARP)是几种染色质重构体的亚基，但它们在这些复合体中的分子功能尚不清楚。我们报道了INO80复合亚单位Arp8以其ATP结合的形式的晶体结构。人类Arp8在保守的肌动蛋白折叠中有几个插入片段，这解释了它无法聚合。最值得注意的是，一个插入物包裹在活性部位裂隙上，似乎使结构域变硬，而与肌动蛋白共享的活性部位特征表明，变构控制的ATPase活性。与核小体和组蛋白复合体的定量结合研究表明，Arp8和INO80的Arp8-Arp4-肌动蛋白-HSA亚复合体强烈地偏好核小体和H3-H4四聚体，而不是H_2A-H_2B二聚体，这表明Arp8作为核小体识别模块发挥作用。相反，Arp4更喜欢游离的(H3-H4)2而不是核小体，并可能通过与重塑反应中的(解离)组装中间体结合来提供重塑。
Nuclear actin-related proteins (Arps) are subunits of several chromatin remodelers, but their molecular functions within these complexes are unclear. We report the crystal structure of the INO80 complex subunit Arp8 in its ATP-bound form. Human Arp8 has several insertions in the conserved actin fold that explain its inability to polymerize. Most remarkably, one insertion wraps over the active site cleft and appears to rigidify the domain architecture, while active site features shared with actin suggest an allosterically controlled ATPase activity. Quantitative binding studies with nucleosomes and histone complexes reveal that Arp8 and the Arp8–Arp4–actin-HSA sub-complex of INO80 strongly prefer nucleosomes and H3–H4 tetramers over H2A–H2B dimers, suggesting that Arp8 functions as a nucleosome recognition module. In contrast, Arp4 prefers free (H3–H4)2 over nucleosomes and may serve remodelers through binding to (dis)assembly intermediates in the remodeling reaction.
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发表时间：
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影响因子：
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