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组蛋白伴侣酵母 Asf1 在组蛋白 H3/H4-DNA 复合物组装和拆卸中的活性。

The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4-DNA complexes.

机构信息

Department of Pharmacology, University of Colorado, School of Medicine, Aurora, CO 80045, USA.

出版信息

Nucleic Acids Res. 2011 Jul;39(13):5449-58. doi: 10.1093/nar/gkr097. Epub 2011 Mar 29.

DOI:10.1093/nar/gkr097
PMID:21447559
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3141235/
Abstract

The deposition of the histones H3/H4 onto DNA to give the tetrasome intermediate and the displacement of H3/H4 from DNA are thought to be the first and the last steps in nucleosome assembly and disassembly, respectively. Anti-silencing function 1 (Asf1) is a chaperone of the H3/H4 dimer that functions in both of these processes. However, little is known about the thermodynamics of chaperone-histone interactions or the direct role of Asf1 in the formation or disassembly of histone-DNA complexes. Here, we show that Saccharomyces cerevisiae Asf1 shields H3/H4 from unfavorable DNA interactions and aids the formation of favorable histone-DNA interactions through the formation of disomes. However, Asf1 was unable to disengage histones from DNA for tetrasomes formed with H3/H4 and strong nucleosome positioning DNA sequences or tetrasomes weakened by mutant (H3K56Q/H4) histones or non-positioning DNA sequences. Furthermore, Asf1 did not associate with preformed tetrasomes. These results are consistent with the measured affinity of Asf1 for H3/H4 dimers of 2.5 nM, which is weaker than the association of H3/H4 for DNA. These studies support a mechanism by which Asf1 aids H3/H4 deposition onto DNA but suggest that additional factors or post-translational modifications are required for Asf1 to remove H3/H4 from tetrasome intermediates in chromatin.

摘要

组蛋白 H3/H4 沉积到 DNA 上形成四聚体中间产物，以及 H3/H4 从 DNA 上置换，分别被认为是核小体组装和拆卸的第一步和最后一步。抗沉默功能 1（Asf1）是 H3/H4 二聚体的伴侣，在这两个过程中都发挥作用。然而，人们对伴侣蛋白-组蛋白相互作用的热力学或 Asf1 在形成或拆开组蛋白-DNA 复合物中的直接作用知之甚少。在这里，我们表明酿酒酵母 Asf1 保护 H3/H4 免受不利的 DNA 相互作用，并通过形成二联体帮助形成有利的组蛋白-DNA 相互作用。然而，Asf1 无法使 H3/H4 与 DNA 分离，对于与 H3/H4 形成的四聚体以及具有强核小体定位 DNA 序列的四聚体或被突变（H3K56Q/H4）组蛋白或非定位 DNA 序列削弱的四聚体。此外，Asf1 与预先形成的四聚体不相关。这些结果与 Asf1 对 H3/H4 二聚体的测量亲和力 2.5 nM 一致，该亲和力弱于 H3/H4 与 DNA 的结合力。这些研究支持了 Asf1 有助于 H3/H4 沉积到 DNA 上的机制，但表明需要其他因素或翻译后修饰才能使 Asf1 从染色质中的四聚体中间体中去除 H3/H4。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/ed0d12622a04/gkr097f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/18466ba63920/gkr097f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/304bcb5f2df3/gkr097f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/8a601c8b0eb5/gkr097f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/ef1ca05b56c1/gkr097f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/ed0d12622a04/gkr097f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/18466ba63920/gkr097f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/304bcb5f2df3/gkr097f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/8a601c8b0eb5/gkr097f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/ef1ca05b56c1/gkr097f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/591b/3141235/ed0d12622a04/gkr097f5.jpg

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