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组蛋白H1序列固有无序特性分析
引用本文:王春玲,于家峰,王红梅,王吉华.组蛋白H1序列固有无序特性分析[J].原子与分子物理学报,2017,34(6).
作者姓名:王春玲  于家峰  王红梅  王吉华
作者单位:德州学院,德州学院,德州学院,德州学院
摘    要:组蛋白H1对于高阶染色质结构的形成和基因表达调控具有重要作用。为了揭示组蛋白H1在染色质结构形成中的生物学机制,本文对组蛋白H1三个结构域C-terminal domain (CTD)、N-terminal domain(NTD)和Globular domain (GD) 及各区域连接位点对应序列氨基酸偏好、复杂度等序列特征进行了系统对比研究,并对各区域进行了固有无序蛋白有序区/无序区预测分析。结果表明,组蛋白H1三个结构中,中间的球状结构域(GD)中的氨基酸序列是非常保守的,NTD富含疏水氨基酸,CTD末端富含碱性氨基酸。进一步的研究表明, CTD和NTD两个结构域普遍具有固有无序特性,因此这些区域具有较大的柔性结构,对其在染色质形成中行使的重要生物学功能具有重要意义。

关 键 词:组蛋白H1  固有无序蛋白  序列分析

Analysis of intrinsically disordered characteristics for histone H1
Abstract:Histone H1 is important both for maintenance of higher-order chromatin structure and for the regulation of gene expression. In this work, in order to reveal the biological mechanism of histone H1 in the formation of chromatin structure, the probability of amino acid, amino acid sequence complexity and the analyzes about junction of three domains are adopted to systematic comprehensive study the sequence features of the three domains(C-terminal domain (CTD), N-terminal domain(NTD) and Globular domain (GD)) of Histone H1, and the ordered / disordered protein region of each sequence is predicted. The results indicate that the amino acid sequence of the globular domain (GD) is highly conserved, NTD is rich in hydrophobic amino acids, and the CTD is rich in basic amino acids, lysine, serine, proline and alanine. Further studies show that CTD and NTD have intrinsically disorder characteristics, so the two regions have a large flexible structure, which can promote them to preform the important biological functions in the formation of the chromatin.
Keywords:Histone H1    Intrinsically disordered protain    Analysis of sequence
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