爱泼斯坦-巴尔病毒核抗原2反式激活结构域的鉴定

Identification of the Epstein-Barr virus nuclear antigen 2 transactivation domain.

作者信息

Horvath G C, Schubach W H

机构信息

Department of Medicine, State University of New York, Stony Brook 11794-8174.

出版信息

Biochem Biophys Res Commun. 1993 Feb 26;191(1):196-200. doi: 10.1006/bbrc.1993.1202.

DOI:10.1006/bbrc.1993.1202

PMID:8383488

Abstract

The Epstein-Barr virus nuclear antigen 2 (EBNA2) protein activates the expression of viral and cellular genes. A set of seven yeast GAL4-EBNA2 fusion proteins were constructed in order to identify the transactivation domain of EBNA2. These fusion proteins were tested for their ability to transactivate a target gene in Hela and BJAB cells. This analysis has demonstrated that the EBNA2 polyproline domain is dispensable for transactivation while the acidic carboxy terminus defined by amino acids 337-467 is essential. This result is consistent with the analysis of a variety of viral and cellular eucaryotic transactivators in which an acidic domain of the protein has been shown to be indispensible for function.

摘要

爱泼斯坦-巴尔病毒核抗原2（EBNA2）蛋白可激活病毒和细胞基因的表达。构建了一组七个酵母GAL4-EBNA2融合蛋白，以鉴定EBNA2的反式激活结构域。测试了这些融合蛋白在Hela细胞和BJAB细胞中反式激活靶基因的能力。该分析表明，EBNA2的多脯氨酸结构域对于反式激活并非必需，而由氨基酸337 - 467定义的酸性羧基末端是必不可少的。这一结果与对多种病毒和细胞真核反式激活因子的分析一致，在这些分析中，蛋白质的酸性结构域已被证明对功能是必不可少的。