Lee W S, Kao C C, Bryant G O, Liu X, Berk A J
Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024-1570.
Cell. 1991 Oct 18;67(2):365-76. doi: 10.1016/0092-8674(91)90188-5.
The adenovirus large E1A protein is a potent activator of transcription. We use several different experimental approaches to demonstrate that the large E1A protein binds specifically and stably to the TATA box-binding factor (TFIID), the general polymerase II transcription factor that initiates assembly of transcription complexes. Sedimentation velocity centrifugation revealed that TFIID and E1A form a heterodimer in vitro. We demonstrate that the activation domain of E1A (conserved region 3) binds to TFIID. E1A interacts with a 51 residue region from the conserved C-terminal domain of TFIID that includes a repeat of basic residues between the homologous direct repeats of TFIID. Analysis of TFIID binding by various E1A mutants indicates that TFIID binding is necessary, although not sufficient, for E1A transactivation.
腺病毒大E1A蛋白是一种强大的转录激活因子。我们采用了几种不同的实验方法来证明大E1A蛋白能特异性且稳定地结合TATA盒结合因子（TFIID），即启动转录复合物组装的通用聚合酶II转录因子。沉降速度离心显示TFIID和E1A在体外形成异二聚体。我们证明E1A的激活结构域（保守区域3）与TFIID结合。E1A与TFIID保守C末端结构域的一个51个残基的区域相互作用，该区域包括TFIID同源直接重复序列之间的一个碱性残基重复序列。对各种E1A突变体与TFIID结合的分析表明，TFIID结合对于E1A反式激活是必要的，尽管不是充分的。
