Deciphering the transcriptional histone acetylation code for a human gene
Deciphering the transcriptional histone acetylation code for a human gene
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DOI：
10.1016/s0092-8674(02)01077-2
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发表时间：
2002-11-01
期刊：
影响因子：
64.5
通讯作者：
Thanos, D
中科院分区：
文献类型：
--
作者：
Agalioti, T;Chen, GY;Thanos, D
我们报告了旨在测试组蛋白密码假说的实验结果。我们发现，只有一小部分的历史H4和H3的赖氨酸在体内乙酰化的GCN 5乙酰转移酶在IFN-β基因的激活过程中。在这些赖氨酸残基中携带突变的重组核小体的重建揭示了通过含溴结构域的转录复合物的有序募集通过逐点解释组蛋白密码的基因激活级联。组蛋白H4和K8的乙酰化介导SWI/SNF复合物的募集，而组蛋白H3中K9和K14的乙酰化对于TFIID的募集至关重要。因此，增强子的DNA地址中包含的信息通过产生转录复合物募集所需的新的粘附表面而转移到组蛋白N末端。
We report the results of experiments designed to test the histone code hypothesis. We found that only a small subset of lysines in histories H4 and H3 are acetylated in vivo by the GCN5 acetyltransferase during activation of the IFN-beta gene. Reconstitution of recombinant nucleosomes bearing mutations in these lysine residues revealed the cascade of gene activation via a point-by-point interpretation of the histone code through the ordered recruitment of bromodomain-containing transcription complexes. Acetylation of histone H4 K8 mediates recruitment of the SWI/SNF complex whereas acetylation of K9 and K14 in histone H3 is critical for the recruitment of TFIID. Thus, the information contained in the DNA address of the enhancer is transferred to the histone N termini by generating novel adhesive surfaces required for the recruitment of transcription complexes.