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Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4

机译:组蛋白伴侣CIA / ASF1与组蛋白H3和H4复合的结构和功能

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摘要

CIA (CCG1 -interacting factor A)/ASF1, which is the most conserved histone chaperone among the eukaryotes, was genetically identified as a factor for an anti-silencing function (Asf1) by yeast genetic screening. Shortly after that, the CIA-histone-H3-H4 complex was isolated from Drosophila as a histone chaperone CAF-1 stimulator. Human CIA-Ⅰ/Ⅱ (ASF1a/b) was identified as a histone chaperone that interacts with the bromodomain—an acetylated-histone-recognizing domain—of CCG1, in the general transcription initiation factor TFIID.
机译:CIA(CCG1-相互作用因子A)/ ASF1是真核生物中最保守的组蛋白分子伴侣,通过酵母基因筛选已被遗传鉴定为抗沉默功能(Asf1)的因子。此后不久,从果蝇中分离出CIA-组蛋白-H3-H4复合物作为组蛋白伴侣CAF-1刺激物。人类CIA-Ⅰ/Ⅱ(ASF1a / b)被鉴定为组蛋白伴侣,它与一般转录起​​始因子TFIID中CCG1的溴结构域(乙酰化组蛋白识别结构域)相互作用。

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