Tora L, White J, Brou C, Tasset D, Webster N, Scheer E, Chambon P
Laboratoire de Génétique Moléculaire des Eucaryotes du CNRS, Unité 184 de Biologie Moléculaire et de Génie Génétique de l'INSERM Institut de Chimie Biologique, Faculté de Médecine, Strasbourg, France.
Cell. 1989 Nov 3;59(3):477-87. doi: 10.1016/0092-8674(89)90031-7.
We have previously reported the presence of a hormone-inducible transcriptional activation function (TAF-2) within the region of the estrogen receptor (ER) that contains the hormone binding domain. We show here that the N-terminal A/B region of the ER contains an independent constitutive activation function (TAF-1) that exhibits cell type specificity since it activates transcription efficiently in chicken embryo fibroblasts, but only poorly in HeLa cells. By analyzing the ability of TAF-1, TAF-2, and the GAL4 and VP16 acidic activating domains (AADs) to homosynergize and heterosynergize with one another and with the factor binding to the upstream element (UE) of the adenovirus 2 major late promoter, we show that the activation properties of TAF-1 and TAF-2 are different and distinct from those of AADs, in agreement with the absence of acidic amino acid stretches in TAF-1 and TAF-2.
我们之前报道过，在雌激素受体（ER）包含激素结合结构域的区域内存在一种激素诱导的转录激活功能（TAF-2）。我们在此表明，ER的N端A/B区域包含一种独立的组成型激活功能（TAF-1），该功能具有细胞类型特异性，因为它在鸡胚成纤维细胞中能有效激活转录，但在HeLa细胞中激活效率很低。通过分析TAF-1、TAF-2以及GAL4和VP16酸性激活结构域（AAD）彼此之间以及与结合腺病毒2主要晚期启动子上游元件（UE）的因子进行同源协同和异源协同的能力，我们发现TAF-1和TAF-2的激活特性与AAD不同，这与TAF-1和TAF-2中不存在酸性氨基酸序列一致。
