人 SUV39H1 chromodomain 的晶体结构及其对组蛋白 H3K9me2/3 的识别。
Crystal structure of the human SUV39H1 chromodomain and its recognition of histone H3K9me2/3.
机构信息
Hefei National Laboratory for Physical Sciences at Microscale, School of Life Science, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
出版信息
PLoS One. 2012;7(12):e52977. doi: 10.1371/journal.pone.0052977. Epub 2012 Dec 28.
SUV39H1, the first identified histone lysine methyltransferase in human, is involved in chromatin modification and gene regulation. SUV39H1 contains a chromodomain in its N-terminus, which potentially plays a role in methyl-lysine recognition and SUV39H1 targeting. In this study, the structure of the chromodomain of human SUV39H1 was determined by X-ray crystallography. The SUV39H1 chromodomain displays a generally conserved structure fold compared with other solved chromodomains. However, different from other chromodomains, the SUV39H1 chromodomain possesses a much longer helix at its C-terminus. Furthermore, the SUV39H1 chromodomain was shown to recognize histone H3K9me2/3 specifically.
SUV39H1 是人类中首个被鉴定的组蛋白赖氨酸甲基转移酶，它参与染色质修饰和基因调控。SUV39H1 在其 N 端含有一个 chromodomain，该结构域可能在识别甲基化赖氨酸和 SUV39H1 的靶向中发挥作用。在本研究中，通过 X 射线晶体学确定了人源 SUV39H1 的 chromodomain 结构。与其他已解析的 chromodomains 相比，SUV39H1 chromodomain 显示出普遍保守的结构折叠。然而，与其他 chromodomains 不同的是，SUV39H1 chromodomain 在其 C 端具有更长的螺旋。此外，SUV39H1 chromodomain 被证明能够特异性地识别组蛋白 H3K9me2/3。
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