Tong X, Wang F, Thut C J, Kieff E
Department of Microbiology, Harvard University, Boston, Massachusetts 02115.
J Virol. 1995 Jan;69(1):585-8. doi: 10.1128/JVI.69.1.585-588.1995.
The Epstein-Barr virus nuclear antigen 2 (EBNA-2) acidic domain is essential for B-lymphocyte growth transformation and can activate transcription when brought to a promoter by a sequence-specific DNA-binding domain. We now show that the EBNA-2 acidic domain has slightly less activity than the proteotypic acidic transactivator VP16 in depleting nuclear extracts of basal transcription activity. Like VP16, EBNA-2 associates with TFIIB, TAF40, and RPA70. However, EBNA-2 has much less avidity for TATA-binding protein. A Trp-to-Thr mutation within the acidic domain abolishes EBNA-2 transactivating activity and greatly compromises the association with TFIIB, TAF40, and RPA70, establishing a genetic linkage between transactivating activity and these associations.
爱泼斯坦-巴尔病毒核抗原2（EBNA-2）酸性结构域对于B淋巴细胞生长转化至关重要，当通过序列特异性DNA结合结构域被带到启动子时，它能够激活转录。我们现在表明，EBNA-2酸性结构域在消耗基础转录活性的核提取物方面，其活性略低于典型酸性反式激活因子VP16。与VP16一样，EBNA-2与TFIIB、TAF40和RPA70相关联。然而，EBNA-2与TATA结合蛋白的亲和力要低得多。酸性结构域内的色氨酸到苏氨酸突变消除了EBNA-2反式激活活性，并极大地损害了与TFIIB、TAF40和RPA70的关联，从而在反式激活活性与这些关联之间建立了遗传联系。
