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Two Distinct Mechanisms of Chromatin Interaction by the Isw2 Chromatin Remodeling Complex In Vivo

机译:Isw2染色质重塑复合物体内染色质相互作用的两种不同机制

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We have previously shown that Saccharomyces cerevisiae Isw2 complex slides nucleosomes to remodel chromatin in vivo. Our data suggested a model in which Isw2 complex binds the histone octamer and DNA separately to generate the force necessary for nucleosome movement. Here we find that the histone H4 “basic patch” is the only portion of any amino-terminal histone tail required for both target-specific association of Isw2 complex with chromatin and chromatin remodeling in vivo, whereas it is dispensable for basal levels of chromatin binding. Similarly, we find that nonremodeled chromatin structure and integrity of Isw2 complex are required only for target-specific association of Isw2 with chromatin. These data demonstrate fundamental differences between the target-specific and basal modes of chromatin binding by Isw2 complex in vivo and suggest that only the former involves contributions from DNA, histone H4, and sequence-specific DNA binding proteins. We propose a model for target recognition and chromatin remodeling by Isw2 complex in vivo.
机译:我们以前已经证明,酿酒酵母 Isw2复合物可在体内塑造核小体来重塑染色质。我们的数据提出了一个模型,其中Isw2复合物分别结合组蛋白八聚体和DNA,以产生核小体移动所需的力。在这里,我们发现组蛋白H4“基本补丁”是Isw2复合物与染色质的靶标特异性结合和染色质重塑在体内都需要的任何氨基末端组蛋白尾巴的唯一部分,而对于染色质结合的基础水平却是必不可少的。同样,我们发现,Isw2与染色质的靶标特异性缔合仅需要非重塑的染色质结构和Isw2复合物的完整性。这些数据证明了Isw2复合物在体内的染色质结合的靶标特异性和基础模式之间的根本区别,并表明只有前者参与了DNA,组蛋白H4和序列特异性DNA结合蛋白的贡献。我们提出了一种在体内通过Isw2复合物进行目标识别和染色质重塑的模型。

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