Structure of the H1 C-terminal domain and function in chromatin condensation.
Structure of the H1 C-terminal domain and function in chromatin condensation.
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DOI：
10.1139/o10-024
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发表时间：
2011-02
期刊：
影响因子：
--
通讯作者：
Hayes JJ
中科院分区：
文献类型：
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作者：
Caterino TL;Hayes JJ
接头组蛋白是多功能蛋白质，其参与从稳定染色质的折叠和凝聚到在调节基因表达中发挥直接作用的无数过程。然而，这类神秘的蛋白质如何结合在染色质中并完成这些功能仍不清楚。在这里，我们回顾有关H1的结构和功能的染色质的数据，特别强调的C-末端结构域（CTD），它通常包括约一半的质量的连接组蛋白，并包括大量过量的带正电荷的残基。由于其氨基酸组成，CTD先前被提出作为非结构化聚阳离子在染色质中起作用。然而，结构研究表明，CTD与DNA和大分子拥挤剂相互作用时采用可检测的二级结构。我们描述了经典和最近的实验定义的功能，这一领域的染色质折叠和新兴的数据表明，这种蛋白质的功能可能与内在的障碍。
Linker histones are multifunctional proteins that are involved in a myriad of processes ranging from stabilizing the folding and condensation of chromatin to playing a direct role in regulating gene expression. However, how this class of enigmatic proteins binds in chromatin and accomplishes these functions remains unclear. Here we review data regarding the H1 structure and function in chromatin, with special emphasis on the C-terminal domain (CTD), which typically encompasses approximately half of the mass of the linker histone and includes a large excess of positively charged residues. Owing to its amino acid composition, the CTD was previously proposed to function in chromatin as an unstructured polycation. However, structural studies have shown that the CTD adopts detectable secondary structure when interacting with DNA and macromolecular crowding agents. We describe classic and recent experiments defining the function of this domain in chromatin folding and emerging data indicating that the function of this protein may be linked to intrinsic disorder.