NuA4 and SWR1-C: two chromatin-modifying complexes with overlapping functions and components

NuA4 and SWR1-C: two chromatin-modifying complexes with overlapping functions and components
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DOI:
10.1139/o09-062
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发表时间:
2009-10-01
影响因子:
2.9
通讯作者:
Kobor, Michael S.
Kobor, Michael S.
中科院分区:
生物学3区
文献类型:
--
作者:
Lu, Phoebe Y. T.;Levesque, Nancy;Kobor, Michael S.

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染色质结构对于真核生物基因组的致密化非常重要,因此染色质修饰在调节许多细胞过程中起着重要作用。各种染色质重塑和修饰复合物的协调活动对于维持不同的染色质邻域至关重要,这反过来又确保了适当的基因表达以及DNA复制、修复和重组。SWR 1-C是组蛋白变体H2A.Z的ATP依赖性组蛋白沉积复合物,而NuA 4是组蛋白H4、H2 A和H2A.Z的历史性乙酰基I转移酶。NuA 4和SWR 1-C染色质修饰复合物一起通过酵母中的3种不同修饰改变染色质结构:翻译后添加化学基团、ATP依赖性染色质重塑和历史变体掺入。这两种多蛋白复合物共有4个亚基,共同发挥调节H2A.Z生物学回路的作用。这两种多蛋白复合物的组成和功能在进化上是保守的,在高等真核生物的多细胞发育和细胞分化中起着重要作用。本文综述了NuA 4和SWR 1-C的最新研究结果,并通过真核生物进化研究它们之间的物理和功能相互作用,重点关注这些复合物之间的联系。
Chromatin structure is important for the compaction of eukaryotic genomes, thus chromatin modifications play a fundamental role in regulating many cellular processes. The coordinated activities of various chromatin-remodelling and-modifying complexes are crucial in maintaining distinct chromatin neighbourhoods, which in turn ensure appropriate gene expression, as well as DNA replication, repair, and recombination. SWR1-C is an ATP-dependent histone deposition complex for the histone variant H2A.Z, whereas NuA4 is a historic acety I transferase for histones H4, H2A, and H2A.Z. Together the NuA4 and SWR1-C chromatin-modifying complexes alter the chromatin structure through 3 distinct modifications in yeast: post-translational addition of chemical groups, ATP-dependent chromatin remodelling, and historic variant incorporation. These 2 multi-protein complexes share 4 subunits and function together to regulate the circuitry of H2A.Z biology. The components and functions of both multi-protein complexes are evolutionarily conserved and play important roles in multi-cellular development and cellular differentiation in higher eukaryotes. This review will summarize recent findings about NuA4 and SWR1-C and will focus on the connection between these complexes by investigating their physical and functional interactions through eukaryotic evolution.