Cell cycle-dependent recruitment of HDAC-1 correlates with deacetylation of histone H4 on an Rb-E2F target promoter
Cell cycle-dependent recruitment of HDAC-1 correlates with deacetylation of histone H4 on an Rb-E2F target promoter
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DOI：
10.1093/embo-reports/kve173
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发表时间：
2001-09-01
期刊：
影响因子：
7.7
通讯作者：
Harel-Bellan, A
中科院分区：
文献类型：
--
作者：
Ferreira, R;Naguibneva, I;Harel-Bellan, A
转录因子E2 F是控制细胞增殖的关键元件，在生长停滞的分化细胞中以及在增殖细胞中，当它们通过早期G时，它被Rb和其他口袋蛋白抑制（1）。目前尚不清楚在这两种情况下是否存在类似的机制。大量数据表明，口袋蛋白的E2 F抑制涉及I类组蛋白脱乙酰酶（HDAC）。据推测，这些酶被募集到E2 F靶启动子，在那里它们使组蛋白脱乙酰化。在这里，我们已经测试了这一假设直接使用甲醛交联染色质免疫沉淀（XChIP）测定，以评估HDAC协会在活细胞。我们的数据表明，组蛋白去乙酰化酶，HDAC-1，是稳定结合到E2 F的目标启动子在早期G，在增殖细胞和释放在G（1）-S转换。此外，我们的研究结果揭示了HDAC-1募集和组蛋白H4乙酰化之间的负相关性的特定赖氨酸。
The transcription factor E2F, which is a key element in the control of cell proliferation, is repressed by Rb and other pocket proteins in growth-arrested differentiating cells, as well as in proliferating cells when they progress through early G(1). It is not known whether similar mechanisms are operative in the two situations. A body of data suggests that E2F repression by pocket proteins involves class I histone deacetylases (HDACs). It has been hypothesized that these enzymes are recruited to E2F target promoters where they deacetylate histones. Here we have tested this hypothesis directly by using formaldehyde cross-linked chromatin immunoprecipitation (XChIP) assays to evaluate HDAC association in living cells. Our data show that a histone deacetylase, HDAC-1, is stably bound to an E2F target promoter during early G, in proliferating cells and released at the G(1)-S transition. In addition, our results reveal an inverse correlation between HDAC-1 recruitment and histone H4 acetylation on specific lysines.