Recruitment of HAT complexes by direct activator interactions with the ATM-related tra1 subunit
Recruitment of HAT complexes by direct activator interactions with the ATM-related tra1 subunit
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DOI：
10.1126/science.1060214
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发表时间：
2001-06-22
期刊：
影响因子：
56.9
通讯作者：
Workman, JL
中科院分区：
文献类型：
--
作者：
Brown, CE;Howe, L;Workman, JL
组蛋白乙酰转移酶活性的启动子特异性募集对于转录激活通常是关键的。我们提出了一个详细的研究组蛋白乙酰转移酶复合物佐贺和NuA4之间的相互作用，和转录激活剂。我们通过亲和层析和光交联标记转移证明，酸性激活剂直接与佐贺和NUA4的共享亚基Tra1p相互作用。Tra1p COOH末端的突变破坏了其与激活剂的相互作用，并导致与启动子特异性组蛋白乙酰化降低相关的基因特异性转录缺陷。这些数据表明，必需的Tra1蛋白作为一个共同的目标，在佐贺和NuA4乙酰转移酶的激活剂。
Promoter-specific recruitment of histone acetyltransferase activity is often critical for transcriptional activation. We present a detailed study of the interaction between the histone acetyltransferase complexes SAGA and NuA4, and transcription activators. We demonstrate by affinity chromatography and photo-cross-linking Label transfer that acidic activators directly interact with Tra1p, a shared subunit of SAGA and NUA4. Mutations within the COOH-terminus of Tra1p disrupted its interaction with activators and resulted in gene-specific transcriptional defects that correlated with Lowered promoter-specific histone acetylation. These data demonstrate that the essential Tra1 protein serves as a common target for activators in both SAGA and NuA4 acetyltransferases.