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首页> 外文期刊>Journal of Molecular Biology >Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM.
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Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM.

机译：RanBPM增强爱泼斯坦-巴尔病毒Rta的反式激活活性。

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Epstein-Barr virus (EBV) expresses the immediate-early protein Rta to activate the transcription of EBV lytic genes and the lytic cycle. We show that RanBPM acts as a binding partner of Rta in yeast two-hybrid analysis. The binding was confirmed by glutathione-S-transferase pull-down assay. A coimmunoprecipitation experiment and confocal microscopy revealed that RanBPM and Rta interact in vivo and colocalize in the nucleus. The interaction appears to involve the SPRY domain in RanBPM and the region between amino acid residues 416 to 476 in Rta. The interaction promotes the transactivation activity of Rta in activating the transcription of BMLF1 and p21 in transient transfection assays. Additionally, RanBPM interacts with SUMO-E2 (Ubc9) to promote sumoylation of Rta by SUMO-1. This fact explains why the expression of RanBPM enhances the transactivation activity of Rta. Taken together, the present results indicate a new role of RanBPM in regulating a viral protein that is critical to EBV lytic activation.
机译：爱泼斯坦巴尔病毒（EBV）表达早期蛋白质Rta，以激活EBV裂解基因的转录和裂解周期。我们表明，RanBPM在酵母双杂交分析中充当Rta的结合伴侣。通过谷胱甘肽-S-转移酶下拉测定法确认结合。一项共免疫沉淀实验和共聚焦显微镜检查显示，RanBPM和Rta在体内相互作用并在细胞核中共定位。相互作用似乎涉及RanBPM中的SPRY结构域和Rta中氨基酸残基416至476之间的区域。在瞬时转染测定中，该相互作用促进Rta激活BMLF1和p21转录的反式激活活性。此外，RanBPM与SUMO-E2（Ubc9）相互作用，以促进SUMO-1对Rta的磺酰化。这个事实解释了为什么RanBPM的表达增强Rta的反式激活活性。两者合计，目前的结果表明RanBPM在调节对EBV裂解激活至关重要的病毒蛋白中的新作用。

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