Histone H4-K16 acetylation controls chromatin structure and protein interactions
Histone H4-K16 acetylation controls chromatin structure and protein interactions
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DOI：
10.1126/science.1124000
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发表时间：
2006-02-10
期刊：
影响因子：
56.9
通讯作者：
Peterson, CL
中科院分区：
文献类型：
--
作者：
Shogren-Knaak, M;Ishii, H;Peterson, CL
组蛋白H4在赖氨酸16上的乙酰化（H4- k16ac）是真核生物中普遍存在的和可逆的翻译后染色质修饰。为了表征该标记的结构和功能作用，我们使用天然化学连接策略生成了在K16处均匀乙酰化的组蛋白H4。将这种修饰的组蛋白整合到核小体阵列中，抑制了致密的30纳米样纤维的形成，并阻碍了染色质形成跨纤维相互作用的能力。H4-K16Ac还抑制三磷酸腺苷利用染色质组装和重塑酶ACF动员单个核小体的能力，表明这种单一组蛋白修饰既可以调节高阶染色质结构，也可以调节非组蛋白与染色质纤维之间的功能相互作用。
Acetylation of histone H4 on lysine 16 (H4-K16Ac) is a prevalent and reversible posttranslational chromatin modification in eukaryotes. To characterize the structural and functional role of this mark, we used a native chemical ligation strategy to generate histone H4 that was homogeneously acetylated at K16. The incorporation of this modified histone into nucleosomal arrays inhibits the formation of compact 30-nanometer-like fibers and impedes the ability of chromatin to form cross-fiber interactions. H4-K16Ac also inhibits the ability of the adenosine triphosphate-utilizing chromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome, indicating that this single histone modification modulates both higher order chromatin structure and functional interactions between a nonhistone protein and the chromatin fiber.