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SWI/SNF复合物的瞬时作用对核小体阵列进行持续的位点特异性重塑。

Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex.

作者信息

Owen-Hughes T, Utley R T, Côté J, Peterson C L, Workman J L

机构信息

Department of Biochemistry and Molecular Biology and Center for Gene Regulation, Pennsylvania State University, University Park, PA 16802-4500, USA.

出版信息

Science. 1996 Jul 26;273(5274):513-6. doi: 10.1126/science.273.5274.513.

DOI:10.1126/science.273.5274.513
PMID:8662543
Abstract

The SWI/SNF complex participates in the restructuring of chromatin for transcription. The function of the yeast SWI/SNF complex in the remodeling of a nucleosome array has now been analyzed in vitro. Binding of the purified SWI/SNF complex to a nucleosome array disrupted multiple nucleosomes in an adenosine triphosphate-dependent reaction. However, removal of SWI/SNF left a deoxyribonuclease I-hypersensitive site specifically at a nucleosome that was bound by derivatives of the transcription factor Gal4p. Analysis of individual nucleosomes revealed that the SWI/SNF complex catalyzed eviction of histones from the Gal4-bound nucleosomes. Thus, the transient action of the SWI/SNF complex facilitated irreversible disruption of transcription factor-bound nucleosomes.

摘要

SWI/SNF复合物参与染色质重构以促进转录。目前已在体外分析了酵母SWI/SNF复合物在核小体阵列重塑中的功能。纯化的SWI/SNF复合物与核小体阵列的结合在依赖三磷酸腺苷的反应中破坏了多个核小体。然而,去除SWI/SNF后,在一个由转录因子Gal4p衍生物结合的核小体处特异性地留下了一个脱氧核糖核酸酶I超敏位点。对单个核小体的分析表明,SWI/SNF复合物催化组蛋白从Gal4结合的核小体上被逐出。因此,SWI/SNF复合物的短暂作用促进了转录因子结合的核小体的不可逆破坏。

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Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex.SWI/SNF复合物的瞬时作用对核小体阵列进行持续的位点特异性重塑。
Science. 1996 Jul 26;273(5274):513-6. doi: 10.1126/science.273.5274.513.
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The interactions of yeast SWI/SNF and RSC with the nucleosome before and after chromatin remodeling.酵母SWI/SNF和RSC在染色质重塑前后与核小体的相互作用。
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Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding.SWI/SNF复合物对核小体核心结构的扰动在其脱离后仍然存在,增强了后续转录因子的结合。
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The yeast SWI-SNF complex facilitates binding of a transcriptional activator to nucleosomal sites in vivo.酵母SWI-SNF复合物在体内促进转录激活因子与核小体位点的结合。
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SWI/SNF stimulates the formation of disparate activator-nucleosome complexes but is partially redundant with cooperative binding.SWI/SNF刺激不同激活因子-核小体复合物的形成,但在协同结合方面存在部分冗余。
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The core histone N-terminal domains are required for multiple rounds of catalytic chromatin remodeling by the SWI/SNF and RSC complexes.核心组蛋白的N端结构域是SWI/SNF和RSC复合物进行多轮催化染色质重塑所必需的。
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The Swi2/Snf2 bromodomain is important for the full binding and remodeling activity of the SWI/SNF complex on H3- and H4-acetylated nucleosomes.Swi2/Snf2溴结构域对于SWI/SNF复合物在H3和H4乙酰化核小体上的完全结合和重塑活性很重要。
Ann N Y Acad Sci. 2008 Sep;1138:366-75. doi: 10.1196/annals.1414.038.

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