Differential remodeling of the HIV-1 nucleosome upon transcription activators and SWI/SNF complex binding
Differential remodeling of the HIV-1 nucleosome upon transcription activators and SWI/SNF complex binding
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DOI：
10.1006/jmbi.2000.4069
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发表时间：
2000-09-15
影响因子：
5.6
通讯作者：
Dimitrov, S
中科院分区：
文献类型：
--
作者：
Angelov, D;Charra, M;Dimitrov, S
在这里，我们已经研究了HIV-1核小体重塑后，结合转录因子和SWI/SNF复合物使用一种新的方法。该方法结合了紫外激光蛋白质-DNA交联，电泳迁移率变化分析和DNase I保护分析与免疫化学技术。结果发现，单个激活剂结合的HIV-1核小体在组蛋白NH 2尾-DNA相互作用中表现出非常弱的扰动。然而，转录激活因子Sp1、NF-kB 1、LEF-1和USF的同时结合协同地增加了组蛋白NH 1尾从核小体DNA的释放。相反，SWI/SNF复合物与HIV-1核小体的结合破坏了结构化的组蛋白结构域-DNA接触，但不破坏组蛋白NH 2尾-DNA相互作用。稳定的重塑核小体（SWI/SNF分离后获得）显示出与SWI/SNF结合的核小体相同的结构改变。这些结果表明，不同的体外重塑的HIV-1核小体后，多种转录激活剂和SWI/SNF复合物的结合。(C)北京大学出版社.
Here we have examined HIV-1 nucleosome remodeling upon the binding of transcription factors and the SWI/SNF complex using a novel approach. The approach combines UV laser protein-DNA crosslinking, electrophoretic mobility-shift analysis and DNase I protection analysis with immunochemical techniques. It was found that single activator-bound HIV-1 nucleosomes exhibit very weak perturbation in histone NH2 tail-DNA interactions. However, the simultaneous binding of the transcription activators Sp1, NF-kB1, LEF-1 and USF synergistically increased the release of histone NH, tails from nucleosomal DNA. In contrast, the binding of SWI/SNF complex to HIV-1 nucleosome disrupted structured histone domain-DNA contacts, but not histone NH2 tail-DNA interactions. Stable remodeled nucleosomes, (obtained after detachment of SWI/SNF), displayed identical structural alterations with those bound to SWI/SNF. These results demonstrate a different in vitro remodeling of the HIV-1 nucleosome upon the binding of multiple transcription activators and of SWI/SNF complex. (C) 2000 Academic Press.