Histone acetylation at promoters is differentially affected by specific activators and repressors
Histone acetylation at promoters is differentially affected by specific activators and repressors
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DOI：
10.1128/mcb.21.8.2726-2735.2001
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发表时间：
2001-04-01
影响因子：
5.3
通讯作者：
Struhl, K
中科院分区：
文献类型：
--
作者：
Deckert, J;Struhl, K
我们分析了组蛋白乙酰化和转录调控之间的关系，在40个酿酒酵母启动子，响应特定的激活剂和抑制剂。与组蛋白乙酰化与转录活性之间的一般相关性雅阁，Gen 4和一般的应激激活因子令人惊讶的是，Cal 1依赖性激活与组蛋白H4乙酰化的显著降低相关，而组蛋白H3的乙酰化不受影响。还观察到H4乙酰化的特异性降低，在较小程度上，在Hap 4、Adr 1、Met 4和Ace 1激活的启动子处。热休克因子的激活具有多种效应; H4乙酰化在一些启动子处增加，而其他启动子显示H3和H4乙酰化明显减少，这可能反映了核小体损失或染色质结构的总体改变。Sin 3-Rpd 3组蛋白去乙酰化酶的靶向募集抑制与H3和H4乙酰化降低相关，而Cyc 8-Tup 1的抑制与H3乙酰化降低相关，但对H3乙酰化的影响不同;这表明Cyc 8-Tup 1使用多种机制来降低启动子处的组蛋白乙酰化。因此，个别激活剂赋予不同模式的组蛋白乙酰化的目标启动子，和转录激活不一定与乙酰化增加，我们推测，激活剂特异性组蛋白H4乙酰化的减少是由于阻止访问或功能的H4特异性组蛋白乙酰化酶，如Esa 1。
We analyzed the relationship between histone acetylation and transcriptional regulation at 40 Saccharomyces cerevisiae promoters that respond to specific activators and repressors. In accord with the general correlation between histone acetylation and transcriptional activity, Gen4 and the general stress activators (Msn2 and Msn4) cause increased acetylation of histones H3 and H4, Surprisingly, Cal 1-dependent activation is associated with a dramatic decrease in histone H4 acetylation, whereas acetylation of histone H3 is unaffected, A specific decrease in H4 acetylation is also observed, to a lesser extent, at promoters activated by Hap4, Adr1, Met4, and Ace1. Activation by heat shock factor has multiple effects; H4 acetylation increases at some promoters, whereas other promoters show an apparent decrease in H3 and H4 acetylation that probably reflects nucleosome loss or gross alteration of chromatin structure. Repression by targeted recruitment of the Sin3-Rpd3 histone deacetylase is associated with decreased H3 and H4 acetylation, whereas repression by Cyc8-Tup1 is associated with decreased H3 acetylation but variable effects on H3 acetylation; this suggests that Cyc8-Tup1 uses multiple mechanisms to reduce histone acetylation at promoters. Thus, individual activators confer distinct patterns of histone acetylation on target promoters, and transcriptional activation is not necessarily associated with increased acetylation, We speculate that the activator-specific decrease in histone H4 acetylation is due to blocking the access or function of an H4-specific histone acetylase such as Esa1.