塑造染色质功能的组蛋白伴侣网络。
Histone chaperone networks shaping chromatin function.
作者信息
Hammond Colin M, Strømme Caroline B, Huang Hongda, Patel Dinshaw J, Groth Anja
机构信息
Biotech Research and Innovation Centre (BRIC) and Centre for Epigenetics, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen DK-2200, Denmark.
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA.
出版信息
Nat Rev Mol Cell Biol. 2017 Mar;18(3):141-158. doi: 10.1038/nrm.2016.159. Epub 2017 Jan 5.
Abstract
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.
摘要
组蛋白与特定伴侣蛋白复合物的结合对于其折叠、寡聚化、翻译后修饰、核输入、稳定性、组装及基因组定位至关重要。通过这种方式，可溶性组蛋白的伴侣作用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、染色体分离以及基因组复制和修复。在此，我们综述了不断扩展的组蛋白伴侣网络的独特结构和功能特性。我们强调了伴侣蛋白如何在组蛋白伴侣网络中以及通过共伴侣蛋白复合物进行协作，以使组蛋白的供应与需求相匹配，从而促进正确的核小体组装，并通过回收从染色质上驱逐的修饰组蛋白来维持表观遗传信息。
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H4K20me0 marks post-replicative chromatin and recruits the TONSL–MMS22L DNA repair complex.H4K20me0标记复制后染色质并招募TONSL–MMS22L DNA修复复合物。
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Nucleosome disassembly during human non-homologous end joining followed by concerted HIRA- and CAF-1-dependent reassembly.人类非同源末端连接过程中的核小体解聚，随后是由HIRA和CAF-1协同依赖的重新组装。
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