Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
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DOI：
10.1016/s0092-8674(00)81063-6
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发表时间：
1996-03-22
期刊：
影响因子：
64.5
通讯作者：
Allis, CD
中科院分区：
文献类型：
--
作者：
Brownell, JE;Zhou, JX;Allis, CD
我们报告的转录相关组蛋白乙酰转移酶A型（HATA）的克隆。这四膜虫酶是惊人的同源酵母蛋白GCN 5，一个假定的转录衔接子，我们证明，重组GCN 5 P具有HAT活性。纤毛虫酶和Gcn 5 p都含有在其他乙酰转移酶中发现的潜在活性位点残基和高度保守的溴结构域。该结构域在核A型HAT中的存在，而不是在细胞质B型HAT中的存在，表明HAT A被定向到染色质以促进转录激活的机制。这些发现揭示了进化上保守的Gcn 5 p-Ada复合物的生物化学功能，直接将组蛋白乙酰化与基因激活联系起来，并表明组蛋白乙酰化是一种靶向现象。
We report the cloning of a transcription-associated histone acetyltransferase type A (HAT A). This Tetrahymena enzyme is strikingly homologous to the yeast protein Gcn5, a putative transcriptional adaptor, and we demonstrate that recombinant Gcn5p possesses HAT activity. Both the ciliate enzyme and Gcn5p contain potential active site residues found in other acetyltransferases and a highly conserved bromodomain. The presence of this domain in nuclear A-type HATs, but not in cytoplasmic B-type HATs, suggests a mechanism whereby HAT A is directed to chromatin to facilitate transcriptional activation. These findings shed light on the biochemical function of the evolutionarily conserved Gcn5p-Ada complex, directly linking histone acetylation to gene activation, and indicate that histone acetylation is a targeted phenomenon.