Yalamanchili R, Tong X, Grossman S, Johannsen E, Mosialos G, Kieff E
Department of Microbiology, Harvard Medical School, Boston, Massachusetts 02115.
Virology. 1994 Nov 1;204(2):634-41. doi: 10.1006/viro.1994.1578.
Epstein-Barr virus (EBV) nuclear protein 2 (EBNA 2) is an acidic transcriptional transactivator of virus and cell gene expression and is essential for growth transformation of primary B lymphocytes. EBNA 2 transactivation of response elements (E2REs) can be mediated by interaction with a GTGGGAA-specific DNA-binding factor(s). We now purify the factor by S-Sepharose and EBNA 2 affinity chromatography and identify it as a single 63-kDa protein. The protein is shown to specifically coimmunoprecipitate with EBNA 2 from lymphoblasts transfected with an EBNA 2 FLAG expression vector. Mutation of GTG to TCT in a GTGGGAA motif common to the Cp, LMP2, and LMP1 promoters results in loss of recognition by p63. EBNA 2 amino acids 310-336 are sufficient for p63 binding. The only motif in this 27 amino acid sequence which is common to the EBNA 2 genes of EBV types 1 and 2 is GPPWWPP (I/V) (C/R) DP, which is therefore likely to mediate p63 interaction. Mutation of WW to SS or FF ablates interaction with p63, indicating that both the hydrophobic and aromatic characteristics of WW are essential for its "key" interaction with p63. EBNA 2 with a WW mutated to SS is also unable to marker rescue primary B lymphocyte transforming virus from cells infected with an EBNA 2-deleted virus, while otherwise isogenic wild-type EBNA 2 readily marker rescues transforming virus in parallel experiments. EBNA 2 transactivation through the Cp E2RE is completely abolished by the WW to SS mutation while transactivation of -234 to +40 LMP1 E2RE is only partially affected. These genetic and biochemical experiments support the hypothesis that EBNA 2 WW interaction with a p63 GTGGGAA-binding protein is essential for EBV-mediated cell growth transformation because it specifically associates EBNA 2 with its response elements. This enables the EBNA 2 acidic domain to transcriptionally transactivate specific genes.
爱泼斯坦-巴尔病毒(EBV)核蛋白2(EBNA 2)是一种酸性转录反式激活因子,可激活病毒和细胞基因表达,对于原代B淋巴细胞的生长转化至关重要。EBNA 2对反应元件(E2REs)的反式激活作用可通过与GTGGGAA特异性DNA结合因子相互作用来介导。我们现在通过S-Sepharose和EBNA 2亲和层析法纯化该因子,并鉴定其为一种单一的63 kDa蛋白。该蛋白显示可与转染了EBNA 2 FLAG表达载体的淋巴母细胞中的EBNA 2特异性共免疫沉淀。在Cp、LMP2和LMP1启动子共有的GTGGGAA基序中,将GTG突变为TCT会导致p63无法识别。EBNA 2的310 - 336位氨基酸足以与p63结合。EBV 1型和2型的EBNA 2基因在这个27个氨基酸序列中唯一共有的基序是GPPWWPP(I/V)(C/R)DP,因此它可能介导与p63的相互作用。将WW突变为SS或FF会消除与p63的相互作用,这表明WW的疏水和芳香特性对于其与p63的“关键”相互作用都至关重要。WW突变为SS的EBNA 2也无法从感染了缺失EBNA 2的病毒的细胞中进行标记拯救原代B淋巴细胞转化病毒,而在平行实验中,其他方面同基因的野生型EBNA 2则很容易进行标记拯救转化病毒。通过Cp E2RE的EBNA 2反式激活作用会因WW突变为SS而完全被消除,而 - 234至 + 40 LMP1 E2RE的反式激活作用仅受到部分影响。这些遗传学和生物化学实验支持了这样一种假说,即EBNA 2的WW与p63 GTGGGAA结合蛋白的相互作用对于EBV介导的细胞生长转化至关重要,因为它使EBNA 2与其反应元件特异性结合。这使得EBNA 2酸性结构域能够转录激活特定基因。