ASF1 binds to a heterodimer of histories H3 and H4: A two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA
ASF1 binds to a heterodimer of histories H3 and H4: A two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA
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DOI：
10.1021/bi051333h
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发表时间：
2005-10-25
期刊：
影响因子：
2.9
通讯作者：
Tyler, JK
中科院分区：
文献类型：
--
作者：
English, CM;Maluf, NK;Tyler, JK
核小体形成的第一步通常被认为是组蛋白H3-H4异源四聚体沉积到DNA上。抗沉默功能I（ASF 1）是一种主要的历史性H3-H4分子伴侣，其将组蛋白H3和H4沉积到DNA上。为了了解组蛋白H3和H4在DNA上沉积的机制，我们确定了Asf 1-H3-H4复合物的化学计量。我们已经建立了一个单一的分子Asf 1结合H3-H4异二聚体使用凝胶过滤，氨基酸，反相色谱，和分析超离心分析。我们表明，Asf 1块H3-H4异源四聚体的形成的机制，可能涉及闭塞的H3-H3二聚化接口。
The first step in the formation of the nucleosome is commonly assumed to be the deposition of a histone H3-H4 heterotetramer onto DNA. Anti silencing function I (ASF1) is a major historic H3-H4 chaperone that deposits histones H3 and H4 onto DNA. With a goal of understanding the mechanism of deposition of histones H3 and H4 onto DNA, we have determined the stoichiometry of the Asf1-H3-H4 complex. We have established that a single molecule of Asf1 binds to an H3-H4 heterodimer using gel filtration, amino acid, reversed-phase chromatography, and analytical ultracentrifugation analyses. We demonstrate that Asf1 blocks formation of the H3-H4 heterotetramer by a mechanism that likely involves occlusion of the H3-H3 dimerization interface.