Biochemical and structural analyses of the nucleosome containing human histone H2A.J
Biochemical and structural analyses of the nucleosome containing human histone H2A.J
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含有人组蛋白 H2A.J 的核小体的生化和结构分析
DOI：
10.1093/jb/mvz109
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发表时间：
2019
期刊：
影响因子：
--
通讯作者：
Kurumizaka Hitoshi
中科院分区：
文献类型：
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作者：
Tanaka Hiroki;Sato Shoko;Koyama Masako;Kujirai Tomoya;Kurumizaka Hitoshi
组蛋白 H2A.J 是哺乳动物中保守的组蛋白 H2A 变体，可能在与炎症和细胞增殖相关的基因表达中发挥作用。在本研究中，我们纯化了人组蛋白H2A.J变体，发现H2A.J在体外能够有效地整合到核小体中。 H2A.J 形成稳定的核小体，容纳 DNA 末端。 H2A.J 特异性残基的突变并不影响核小体稳定性，尽管在经典 H2A 类的一些成员中保守的 H2A.J Ala40 残基的突变降低了核小体稳定性。一致地，H2A.J核小体的晶体结构揭示H2A.J特异性残基，包括Ala40残基，不影响核小体结构。这些结果为理解 H2A.J 核小体的功能提供了基础信息。
Histone H2A.J, a histone H2A variant conserved in mammals, may function in the expression of genes related to inflammation and cell proliferation. In the present study, we purified the human histone H2A.J variant and found that H2A.J is efficiently incorporated into the nucleosomein vitro. H2A.J formed the stable nucleosome, which accommodated the DNA ends. Mutations in the H2A.J-specific residues did not affect the nucleosome stability, although the mutation of the H2A.J Ala40 residue, which is conserved in some members of the canonical H2A class, reduced the nucleosome stability. Consistently, the crystal structure of the H2A.J nucleosome revealed that the H2A.J-specific residues, including the Ala40 residue, did not affect the nucleosome structure. These results provide basic information for understanding the function of the H2A.J nucleosome.