Department of Biochemistry, University of Cambridge, Cambridge, UK.
Nat Struct Mol Biol. 2013 Jan;20(1):29-35. doi: 10.1038/nsmb.2446. Epub 2012 Nov 25.
The mechanisms by which histones are disassembled and reassembled into nucleosomes and chromatin structure during DNA replication, repair and transcription are poorly understood. A better understanding of the processes involved is, however, crucial if we are to understand whether and how histone variants and post-translationally modified histones are inherited in an epigenetic manner. To this end we have studied the interaction of the histone H3-H4 complex with the human retinoblastoma-associated protein RbAp48 and their exchange with a second histone chaperone, anti-silencing function protein 1 (ASF1). Exchange of histones H3-H4 between these two histone chaperones has a central role in the assembly of new nucleosomes, and we show here that the H3-H4 complex has an unexpected structural plasticity, which is important for this exchange.
组蛋白在 DNA 复制、修复和转录过程中如何解组装和再组装成核小体和染色质结构，目前人们对此知之甚少。然而，如果我们要了解组蛋白变体和翻译后修饰的组蛋白是否以及如何以表观遗传方式遗传，那么更好地理解所涉及的过程至关重要。为此，我们研究了组蛋白 H3-H4 复合物与人类视网膜母细胞瘤相关蛋白 RbAp48 的相互作用及其与第二种组蛋白伴侣 ASF1 的交换。这两种组蛋白伴侣之间的 H3-H4 交换在新核小体的组装中起着核心作用，我们在这里表明，H3-H4 复合物具有出人意料的结构可塑性，这对于这种交换很重要。
