Divergent hTAFII31-binding motifs hidden in activation domains
Divergent hTAFII31-binding motifs hidden in activation domains
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DOI：
10.1074/jbc.275.21.15912
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发表时间：
2000-05-26
影响因子：
4.8
通讯作者：
Uesugi, M
中科院分区：
文献类型：
--
作者：
Choi, Y;Asada, S;Uesugi, M
激活域是使 DNA 结合蛋白能够刺激转录的功能模块。转录因子中这些重要模块的表征因其低序列同源性而受到阻碍。在这里，我们描述了反式激活和与 hTAF(II)31 相互作用所需的肽序列，hTAF(II)31 是酸性类激活结构域的经典靶标。我们的分析表明 hTAF(II)31 识别一组不同的反式激活序列。这些信息使得能够鉴定 hTAF(II) 31 结合序列，这些序列对于五种人类转录因子（NFAT1、ALL1、NF-IL6、ESX 和 HSF-1）激活域的活性至关重要。相互作用表面位于激活域的短肽片段中。基序的简洁性和异质性可以解释酸性激活结构域之间的低序列同源性。
Activation domains are functional modules that enable DNA-binding proteins to stimulate transcription. Characterization of these essential modules in transcription factors has been hampered by their low sequence homology. Here we delineate the peptide sequences that are required for transactivation and interaction with hTAF(II)31, a classical target of the acidic class of activation domains. Our analyses indicate that hTAF(II)31 recognizes a diverse set of sequences for transactivation. This information enabled the identification of hTAF(II) 31-binding sequences that are critical for the activity of the activation domains of five human transcription factors: NFAT1, ALL1, NF-IL6, ESX, and HSF-1. The interaction surfaces are localized in short peptide segments of activation domains. The brevity and heterogeneity of the motifs may explain the low sequence homology among acidic activation domains.