首页> 美国卫生研究院文献>Journal of Virology >ICP27 Recruits Aly/REF but Not TAP/NXF1 to Herpes Simplex Virus Type 1 Transcription Sites although TAP/NXF1 Is Required for ICP27 Export
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ICP27 Recruits Aly/REF but Not TAP/NXF1 to Herpes Simplex Virus Type 1 Transcription Sites although TAP/NXF1 Is Required for ICP27 Export

机译:ICP27招募Aly / REF而非TAP / NXF1招募单纯疱疹病毒1型转录位点尽管ICP27导出需要TAP / NXF1

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摘要

Herpes simplex virus type 1 (HSV-1) protein ICP27 interacts with the cellular export adaptor protein Aly/REF, which is part of the exon junction complex implicated in cellular mRNA export. We previously reported that Aly/REF was no longer associated with splicing factor SC35 sites during infection but instead colocalized with ICP27 in distinct structures. Here we show that these structures colocalize with ICP4 and are sites of HSV-1 transcription. ICP27 mutants with lesions in the region required for the interaction with Aly/REF failed to recruit Aly/REF to viral transcription sites; however, ICP27 export to the cytoplasm was unimpaired, indicating that the interaction of ICP27 with Aly/REF is not required for ICP27 shuttling. ICP27 has also been shown to interact with the cellular mRNA export receptor TAP/NXF1. We report that ICP27 interacts directly with TAP/NXF1 and does not require Aly/REF to bridge the interaction. The C terminus of ICP27 is required; however, the N-terminal leucine-rich region also contributes to the interaction of ICP27 with TAP/NXF1. In contrast to the results found for Aly/REF, mutants that failed to interact with TAP/NXF1 were not exported to the cytoplasm, and TAP/NXF1 was not recruited to sites of HSV-1 transcription. Therefore, the interaction of ICP27 with TAP/NXF1 occurs after ICP27 leaves viral transcription sites. We conclude that ICP27 and the viral RNAs to which it binds are exported via the TAP/NXF1 export receptor.
机译:单纯疱疹病毒1型(HSV-1)蛋白ICP27与细胞输出衔接蛋白Aly / REF相互作用,这是与细胞mRNA输出有关的外显子连接复合体的一部分。我们先前曾报道,Aly / REF在感染过程中不再与剪接因子SC35位点相关,而是与ICP27共同定位在不同的结构中。在这里,我们显示这些结构与ICP4共定位,并且是HSV-1转录的位点。在与Aly / REF相互作用所需区域具有病变的ICP27突变体无法将Aly / REF募集到病毒转录位点;但是,ICP27到细胞质的出口没有受到损害,这表明ICP27穿梭不需要ICP27与Aly / REF的相互作用。 ICP27也已显示与细胞mRNA输出受体TAP / NXF1相互作用。我们报告ICP27直接与TAP / NXF1交互,不需要Aly / REF桥接交互。需要ICP27的C端;但是,富含N末端亮氨酸的区域也有助于ICP27与TAP / NXF1的相互作用。与Aly / REF的结果相反,未能与TAP / NXF1相互作用的突变体不会输出到细胞质,而TAP / NXF1也不会募集到HSV-1转录位点。因此,ICP27离开病毒转录位点后,发生ICP27与TAP / NXF1的相互作用。我们得出的结论是,ICP27及其结合的病毒RNA通过TAP / NXF1出口受体出口。

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