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CAF-1 诱导组蛋白 H3/H4 寡聚化和与 Asf1 的相互排斥相互作用，指导 H3/H4 在组蛋白伴侣和 DNA 之间的转变。

CAF-1-induced oligomerization of histones H3/H4 and mutually exclusive interactions with Asf1 guide H3/H4 transitions among histone chaperones and DNA.

机构信息

Department of Pharmacology, University of Colorado School of Medicine, Mail Stop 8303, PO Box 6511, Aurora, CO 80045, USA.

出版信息

Nucleic Acids Res. 2012 Dec;40(22):11229-39. doi: 10.1093/nar/gks906. Epub 2012 Oct 2.

DOI:10.1093/nar/gks906
PMID:23034810
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3526290/
Abstract

Anti-silencing function 1 (Asf1) and Chromatin Assembly Factor 1 (CAF-1) chaperone histones H3/H4 during the assembly of nucleosomes on newly replicated DNA. To understand the mechanism of histone H3/H4 transfer among Asf1, CAF-1 and DNA from a thermodynamic perspective, we developed and employed biophysical approaches using full-length proteins in the budding yeast system. We find that the C-terminal tail of Asf1 enhances the interaction of Asf1 with CAF-1. Surprisingly, although H3/H4 also enhances the interaction of Asf1 with the CAF-1 subunit Cac2, H3/H4 forms a tight complex with CAF-1 exclusive of Asf1, with an affinity weaker than Asf1-H3/H4 or H3/H4-DNA interactions. Unlike Asf1, monomeric CAF-1 binds to multiple H3/H4 dimers, which ultimately promotes the formation of (H3/H4)(2) tetramers on DNA. Thus, transition of H3/H4 from the Asf1-associated dimer to the DNA-associated tetramer is promoted by CAF-1-induced H3/H4 oligomerization.

摘要

抗沉默功能 1（Asf1）和染色质组装因子 1（CAF-1）在新复制的 DNA 上组装核小体时，作为组蛋白 H3/H4 的伴侣。为了从热力学角度理解组蛋白 H3/H4 在 Asf1、CAF-1 和 DNA 之间转移的机制，我们在芽殖酵母系统中使用全长蛋白开发并采用了生物物理方法。我们发现 Asf1 的 C 端尾巴增强了 Asf1 与 CAF-1 的相互作用。令人惊讶的是，尽管 H3/H4 也增强了 Asf1 与 CAF-1 亚基 Cac2 的相互作用，但 H3/H4 与 CAF-1 形成了一个紧密的复合物，不包含 Asf1，其亲和力弱于 Asf1-H3/H4 或 H3/H4-DNA 相互作用。与 Asf1 不同，单体 CAF-1 结合多个 H3/H4 二聚体，最终促进（H3/H4）2 四聚体在 DNA 上的形成。因此，H3/H4 从 Asf1 相关二聚体向 DNA 相关四聚体的转变是由 CAF-1 诱导的 H3/H4 寡聚化促进的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/97022dd937ca/gks906f6p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/318547d18989/gks906f1p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/a07f8cc4559e/gks906f2p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/b2626ec9e1c5/gks906f3p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/06fb374efea9/gks906f4p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/b54d1b2cd2e6/gks906f5p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/97022dd937ca/gks906f6p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/318547d18989/gks906f1p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/a07f8cc4559e/gks906f2p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/b2626ec9e1c5/gks906f3p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/06fb374efea9/gks906f4p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/b54d1b2cd2e6/gks906f5p.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dd21/3526290/97022dd937ca/gks906f6p.jpg

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