Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.
Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.
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DOI：
10.1016/j.jmb.2017.06.005
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发表时间：
2017-08-04
影响因子：
5.6
通讯作者：
Shechter D
中科院分区：
文献类型：
--
作者：
Warren C;Shechter D
染色质是真核生物DNA和蛋白质的复合体，是将近两米长的人类基因组有效压缩成直径约10微米的细胞核所必需的。染色质的基本重复单位是核小体：147bp的DNA包裹在组蛋白的八聚体上。核小体足够稳定，可以组织基因组，但必须动态移位和重组，才能接触到潜在的DNA，进行转录、复制和DNA损伤修复。组蛋白伴侣是一组非催化性蛋白质，对核小体组装和拆卸过程至关重要，因此对不断变化的染色质景观的流动性至关重要。组蛋白伴侣负责结合高度碱性的组蛋白，保护它们免受非特异性相互作用，促进它们沉积到DNA上，并帮助它们从DNA中移除。尽管大多数组蛋白伴侣具有这些共同的功能，但最近对许多不同组蛋白伴侣的结构研究表明，它们的折叠几乎没有共同点。重要的是，基于序列的预测表明，组蛋白伴侣蛋白在内在无序区（idr）和酸性延伸区高度富集。在这篇综述中，我们将重点关注组蛋白结合、选择性和这些高动态蛋白区域的调控的分子机制。我们强调了新的证据表明idr通常对组蛋白伴侣的功能至关重要，并在染色质组装和拆卸途径中发挥关键作用。
Chromatin is the complex of eukaryotic DNA and proteins required for the efficient compaction of the nearly two-meter long human genome into a roughly ten-micron diameter cell nucleus. The fundamental repeating unit of chromatin is the nucleosome: 147bp of DNA wrapped about an octamer of histone proteins. Nucleosomes are stable enough to organize the genome yet must be dynamically displaced and reassembled to allow access to the underlying DNA for transcription, replication, and DNA damage repair. Histone chaperones are a non-catalytic group of proteins that are central to the processes of nucleosome assembly and disassembly, and thus the fluidity of the ever-changing chromatin landscape. Histone chaperones are responsible for binding the highly basic histone proteins, shielding them from non-specific interactions, facilitating their deposition onto DNA, and aiding in their eviction from DNA. Though most histone chaperones perform these common functions, recent structural studies of many different histone chaperones reveal that there are few commonalities in their folds. Importantly, sequence-based predictions show that histone chaperones are highly enriched in intrinsically disordered regions (IDRs) and acidic stretches. In this review, we focus on the molecular mechanisms underpinning histone binding, selectivity, and regulation of these highly dynamic protein regions. We highlight new evidence suggesting that IDRs are often critical for histone chaperone function and play key roles in chromatin assembly and disassembly pathways.
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