Boyne James R, Colgan Kevin J, Whitehouse Adrian
Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
PLoS Pathog. 2008 Oct;4(10):e1000194. doi: 10.1371/journal.ppat.1000194. Epub 2008 Oct 31.
A cellular pre-mRNA undergoes various post-transcriptional processing events, including capping, splicing and polyadenylation prior to nuclear export. Splicing is particularly important for mRNA nuclear export as two distinct multi-protein complexes, known as human TREX (hTREX) and the exon-junction complex (EJC), are recruited to the mRNA in a splicing-dependent manner. In contrast, a number of Kaposi's sarcoma-associated herpesvirus (KSHV) lytic mRNAs lack introns and are exported by the virus-encoded ORF57 protein. Herein we show that ORF57 binds to intronless viral mRNAs and functions to recruit the complete hTREX complex, but not the EJC, in order assemble an export component viral ribonucleoprotein particle (vRNP). The formation of this vRNP is mediated by a direct interaction between ORF57 and the hTREX export adapter protein, Aly. Aly in turn interacts directly with the DEAD-box protein UAP56, which functions as a bridge to recruit the remaining hTREX proteins to the complex. Moreover, we show that a point mutation in ORF57 which disrupts the ORF57-Aly interaction leads to a failure in the ORF57-mediated recruitment of the entire hTREX complex to the intronless viral mRNA and inhibits the mRNAs subsequent nuclear export and virus replication. Furthermore, we have utilised a trans-dominant Aly mutant to prevent the assembly of the complete ORF57-hTREX complex; this results in a vRNP consisting of viral mRNA bound to ORF57, Aly and the nuclear export factor, TAP. Strikingly, although both the export adapter Aly and the export factor TAP were present on the viral mRNP, a dramatic decrease in intronless viral mRNA export and virus replication was observed in the absence of the remaining hTREX components (UAP56 and hTHO-complex). Together, these data provide the first direct evidence that the complete hTREX complex is essential for the export of KSHV intronless mRNAs and infectious virus production.
细胞前体mRNA在核输出之前会经历各种转录后加工事件,包括加帽、剪接和聚腺苷酸化。剪接对于mRNA核输出尤为重要,因为两种不同的多蛋白复合物,即人类转录-输出衔接子(hTREX)和外显子连接复合物(EJC),会以剪接依赖的方式被招募到mRNA上。相比之下,许多卡波西肉瘤相关疱疹病毒(KSHV)的裂解性mRNA缺乏内含子,并由病毒编码的ORF57蛋白输出。在此我们表明,ORF57与无内含子的病毒mRNA结合,并发挥作用招募完整的hTREX复合物,但不招募EJC,以便组装一个输出成分病毒核糖核蛋白颗粒(vRNP)。这种vRNP的形成是由ORF57与hTREX输出衔接蛋白Aly之间的直接相互作用介导的。Aly反过来又直接与DEAD盒蛋白UAP56相互作用,UAP56起到桥梁作用,将其余的hTREX蛋白招募到复合物中。此外,我们表明ORF57中的一个点突变破坏了ORF57-Aly相互作用,导致ORF57介导的将整个hTREX复合物招募到无内含子病毒mRNA的过程失败,并抑制了mRNA随后的核输出和病毒复制。此外,我们利用了一个反式显性Aly突变体来阻止完整的ORF57-hTREX复合物的组装;这导致形成一个由与ORF57、Aly和核输出因子TAP结合的病毒mRNA组成的vRNP。引人注目的是,尽管输出衔接蛋白Aly和输出因子TAP都存在于病毒mRNP上,但在没有其余hTREX成分(UAP56和hTHO复合物)的情况下,观察到无内含子病毒mRNA输出和病毒复制显著减少。总之,这些数据提供了首个直接证据,表明完整的hTREX复合物对于KSHV无内含子mRNA的输出和传染性病毒的产生至关重要。