THE ADENOVIRUS MAJOR LATE TRANSCRIPTION FACTOR USF IS A MEMBER OF THE HELIX LOOP HELIX GROUP OF REGULATORY PROTEINS AND BINDS TO DNA AS A DIMER
THE ADENOVIRUS MAJOR LATE TRANSCRIPTION FACTOR USF IS A MEMBER OF THE HELIX LOOP HELIX GROUP OF REGULATORY PROTEINS AND BINDS TO DNA AS A DIMER
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DOI：
10.1101/gad.4.10.1730
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发表时间：
1990-10-01
影响因子：
10.5
通讯作者：
ROEDER, RG
中科院分区：
文献类型：
--
作者：
GREGOR, PD;SAWADOGO, M;ROEDER, RG
我们分离全长cDNA编码的43 kD形式的人上游刺激因子（USF），所需的腺病毒主要晚期（AdML）启动子在体外有效转录的细胞因子。序列分析表明USF是c-myc相关的DNA结合蛋白家族的成员。使用在体外翻译的蛋白质，我们确定了一个DNA结合结构域附近的羧基末端，其中包括一个螺旋-环-螺旋基序和亮氨酸重复。我们表明，USF与其靶DNA作为二聚体相互作用。亮氨酸重复序列是完整蛋白质的有效DNA结合以及全长和截短的USAF蛋白质之间的相互作用所必需的。有趣的是，分离的螺旋-环-螺旋结构域的DNA结合不需要它。不同cDNA克隆的结构表明USF RNA是差异剪接的，并且选择性外显子的使用可能调节功能性USF蛋白的水平。
We isolated full-length cDNAs encoding the 43-kD form of human upstream stimulatory factor (USF), a cellular factor required for efficient transcription of the adenovirus major late (AdML) promoter in vitro. Sequence analysis showed USF to be a member of the c-myc-related family of DNA-binding proteins. Using proteins translated in vitro, we identified a DNA-binding domain near the carboxyl terminus, which includes both a helix-loop-helix motif and a leucine repeat. We show that USF interacts with its target DNA as a dimer. The leucine repeat is required for efficient DNA binding of the intact protein and for interactions between full-length and truncated USAF proteins. Interestingly, it is not required for DNA binding of the isolated helix-loop-helix domain. The structure of different cDNA clones indicates that USF RNA is differentially spliced, and alternative exon usage may regulate the levels of functional USF protein.