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组蛋白首先发生高度乙酰化,然后与激活的PHO5启动子失去接触。

Histones are first hyperacetylated and then lose contact with the activated PHO5 promoter.

作者信息

Reinke Hans, Hörz Wolfram

机构信息

Molekularbiologie, Adolf-Butenandt-Institut, Universität München, Schillerstrasse 44, D-80336 Münich, Germany.

出版信息

Mol Cell. 2003 Jun;11(6):1599-607. doi: 10.1016/s1097-2765(03)00186-2.

Abstract

We have analyzed the histone modification status of the PHO5 promoter from yeast by the ChIP technology and have focused on changes occurring upon activation. Using various acetylation-specific antibodies, we found a dramatic loss of the acetylation signal upon induction of the promoter. This turned out to be due, however, to the progressive loss of histones altogether. The fully remodeled promoter appears to be devoid of histones as judged by ChIP analyses. Local histone hyperacetylation does indeed occur, however, prior to remodeling. This can explain the delay in chromatin remodeling in the absence of histone acetyltransferase activity of the SAGA complex that was previously documented for the PHO5 promoter. Our findings shed new light on the nucleosomal structure of fully remodeled chromatin. At the same time, they point out the need for novel controls when the ChIP technique is used to study histone modifications in the context of chromatin remodeling in vivo.

摘要

我们通过染色质免疫沉淀(ChIP)技术分析了酵母中PHO5启动子的组蛋白修饰状态,并重点研究了激活过程中发生的变化。使用各种乙酰化特异性抗体,我们发现启动子诱导后乙酰化信号急剧丧失。然而,事实证明这完全是由于组蛋白的逐渐丧失。通过ChIP分析判断,完全重塑的启动子似乎不含组蛋白。不过,在重塑之前确实发生了局部组蛋白高度乙酰化。这可以解释先前记录的PHO5启动子在缺乏SAGA复合物组蛋白乙酰转移酶活性时染色质重塑的延迟。我们的发现为完全重塑的染色质的核小体结构提供了新的见解。同时,它们指出在体内染色质重塑背景下使用ChIP技术研究组蛋白修饰时需要新的对照。

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