Histone chaperone networks shaping chromatin function.
Histone chaperone networks shaping chromatin function.
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DOI：
10.1038/nrm.2016.159
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发表时间：
2017-03
期刊：
影响因子：
--
通讯作者：
Groth A
中科院分区：
文献类型：
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作者：
Hammond CM;Strømme CB;Huang H;Patel DJ;Groth A
组蛋白与特定伴侣复合物的关联对于它们的折叠、寡聚化、翻译后修饰、核导入、稳定性、组装和基因组定位是重要的。通过这种方式，可溶性组蛋白的陪伴是组蛋白可用性和命运的关键决定因素，它影响所有染色体过程，包括基因表达、染色体分离和基因组复制和修复。在这里，我们回顾了组蛋白伴侣蛋白扩展网络的独特结构和功能特性。我们强调伴侣如何在组蛋白伴侣网络中合作，并通过共同伴侣复合物匹配组蛋白供需，从而促进核小体的适当组装，并通过回收从染色质中驱逐的修饰组蛋白来维持表观遗传信息。组蛋白伴侣保护染色质模板，保护组蛋白免受混杂相互作用，以确保其适当的储存、运输、翻译后修饰、核小体组装和周转。
The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble histones is a key determinant of histone availability and fate, which affects all chromosomal processes, including gene expression, chromosome segregation and genome replication and repair. Here, we review the distinct structural and functional properties of the expanding network of histone chaperones. We emphasize how chaperones cooperate in the histone chaperone network and via co-chaperone complexes to match histone supply with demand, thereby promoting proper nucleosome assembly and maintaining epigenetic information by recycling modified histones evicted from chromatin. Histone chaperones safeguard the chromatin template and shield histones from promiscuous interactions to ensure their proper storage, transport, post-translational modification, nucleosome assembly and turnover.