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重新审视 Polycomb 组蛋白对染色质的压缩。

Chromatin compaction by Polycomb group proteins revisited.

机构信息

Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, Victoria, 3800, Australia.

Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, Victoria, 3800, Australia; EMBL-Australia, Clayton, Victoria, 3800, Australia.

出版信息

Curr Opin Struct Biol. 2024 Jun;86:102806. doi: 10.1016/j.sbi.2024.102806. Epub 2024 Mar 27.

Abstract

The chromatin compaction activity of Polycomb group proteins has traditionally been considered essential for transcriptional repression. However, there is very little information on how Polycomb group proteins compact chromatin at the molecular level and no causal link between the compactness of chromatin and transcriptional repression. Recently, a more complete picture of Polycomb-dependent chromatin architecture has started to emerge, owing to advanced methods for imaging and chromosome conformation capture. Discoveries into Polycomb-driven phase separation add another layer of complexity. Recent observations generally imply that Polycomb group proteins modulate chromatin structure at multiple scales to reduce its dynamics and segregate it from active domains. Hence, it is reasonable to hypothesise that Polycomb group proteins maintain the energetically favourable state of compacted chromatin, rather than actively compact it.

摘要

多梳蛋白复合物的染色质紧缩活性传统上被认为对转录抑制至关重要。然而,关于多梳蛋白复合物如何在分子水平上紧缩染色质,以及染色质的紧缩程度与转录抑制之间是否存在因果关系,信息非常有限。最近,由于用于成像和染色体构象捕获的先进方法,多梳蛋白依赖性染色质结构的更完整图景开始显现。多梳蛋白驱动的相分离的发现增加了另一层复杂性。最近的观察结果通常表明,多梳蛋白复合物在多个尺度上调节染色质结构,以降低其动力学并将其与活性区域隔离开来。因此,合理的假设是多梳蛋白复合物维持紧缩染色质的有利能状态,而不是主动紧缩它。

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