A putative DNA binding surface in the globular domain of a linker histone is not essential for specific binding to the nucleosome
A putative DNA binding surface in the globular domain of a linker histone is not essential for specific binding to the nucleosome
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DOI：
10.1074/jbc.271.42.25817
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发表时间：
1996-10-18
影响因子：
4.8
通讯作者：
Wolffe, A
中科院分区：
文献类型：
--
作者：
Hayes, JJ;Kaplan, R;Wolffe, A
天然染色质组装的基本步骤是连接组蛋白与称为核小体的核蛋白亚基的特异性识别和结合。定义这种重要相互作用的第一步是确定连接体组蛋白中对核小体核心的结构特异性识别很重要的残基。通过结合体外试验的天然结合活性的连接组蛋白和定点诱变，我们已经检查了一个集群的碱性残基的球状结构域的H1（0），体细胞连接组蛋白变异体非洲爪蟾。我们表明，这些残基，其中包括一个假定的DNA结合表面内的球状域，不发挥重要作用的结构特异性结合的接头组蛋白的核小体。
A fundamental step in the assembly of native chromatin is the specific recognition and binding of linker histones to the nucleoprotein subunit known as the nucleosome. A first step in defining this important interaction is the determination of residues within Linker histones that are important for the structure-specific recognition of the nucleosome core. By combining in vitro assays for the native binding activity of linker histones and site-directed mutagenesis, we have examined a cluster of basic residues within the globular domain of H1(0), a somatic Linker histone variant from Xenopus laevis. We show that these residues, which comprise a putative DNA binding surface within the globular domain, do not play an essential role in the structure-specific binding of a linker histone to the nucleosome.