Suppr超能文献

爱泼斯坦-巴尔病毒核蛋白2酸性结构域可与TFIIB、TAF40和RPA70相互作用,但不与TATA结合蛋白相互作用。

The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein.

作者信息

Tong X, Wang F, Thut C J, Kieff E

机构信息

Department of Microbiology, Harvard University, Boston, Massachusetts 02115.

出版信息

J Virol. 1995 Jan;69(1):585-8. doi: 10.1128/JVI.69.1.585-588.1995.

Abstract

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.

摘要

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。

相似文献

引用本文的文献

4
Critical Involvement of TFIIB in Viral Pathogenesis.TFIIB在病毒致病机制中的关键作用。
Front Mol Biosci. 2021 Apr 30;8:669044. doi: 10.3389/fmolb.2021.669044. eCollection 2021.
10
BS69/ZMYND11 C-Terminal Domains Bind and Inhibit EBNA2.BS69/ZMYND11的C末端结构域结合并抑制EBNA2。
PLoS Pathog. 2016 Feb 4;12(2):e1005414. doi: 10.1371/journal.ppat.1005414. eCollection 2016 Feb.

本文引用的文献

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验