The HMGB1 acidic tail regulates HMGB1 DNA binding specificity by a unique mechanism
The HMGB1 acidic tail regulates HMGB1 DNA binding specificity by a unique mechanism
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DOI：
10.1016/j.bbrc.2007.05.130
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发表时间：
2007-08-17
影响因子：
3.1
通讯作者：
Tang, Jie
中科院分区：
文献类型：
--
作者：
Wang, Qiyu;Zeng, Minghui;Tang, Jie
HMGB1是一种保守的染色体蛋白，由两个dna结合结构域和一个酸性c端尾部组成。有证据表明，c端尾巴对n端DNA结合域的DNA结合特异性有贡献。然而，这一观察结果背后的机制在很大程度上是未知的。我们的数据首先证实了之前的核磁共振研究，表明HMGB1的c端尾部与其n端结构域之间存在直接相互作用。我们进一步证明，与线性双链DNA相比，具有四向结结构的DNA可以更有效地竞争这种相互作用。n端区域的突变破坏了其与c端尾部的结合，破坏了HMGB1区分线性DNA和四向连接DNA的能力。这些数据表明，自然界设计了一种独特的机制，利用蛋白质的带负电荷的c端尾部来增强其dna结合域对某些结构dna的特异性。(c) 2007年Elsevier Inc.出版
HMGB1 is a conserved chromosomal protein composed of two DNA-binding domains and an acidic C-terminal tail. There were evidences suggesting that the C-terminal tail contributed to the DNA binding specificity of the N-terminal DNA-binding domains. However, the mechanism underlining this observation is largely unknown. Our data first confirmed the previous study with NMR that showed a direct interaction between HMGB1's C-terminal tail and its N-terminal domains. We further demonstrated that this interaction can be competed more efficiently by a DNA with four-way junction structure than by a linear double-stranded DNA. Mutations within the N-terminal region, that disrupt its binding to the C-terminal tail, abolished HMGB1's ability to distinguish the linear DNA and the four-way junction DNA. Those data suggested a unique mechanism designed by nature that utilizes a protein's negatively charged C-terminal tail to enhance its DNA-binding domain's specificity to certain structured DNAs. (c) 2007 Published by Elsevier Inc.