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Influenza A virus NS1 protein binds as a dimer to the RNA-free PABP1 but not to the PABP1-Poly(A) RNA Complex
bioRxiv - Biochemistry Pub Date : 2020-08-10 , DOI: 10.1101/2020.08.10.245225
Cyrus M de Rozières , Simpson Joseph

Influenza A virus (IAV) is a highly contagious human pathogen responsible for nearly half a million deaths each year. Non-structural protein 1 (NS1) is a crucial protein expressed by IAV to evade the host immune system. Additionally, NS1 has been proposed to stimulate translation because of its ability to bind poly(A) binding protein 1 (PABP1) and eukaryotic initiation factor 4G (eIF4G). We analyzed the interaction of NS1 with PABP1 using quantitative techniques. Our studies show that NS1 binds as a homodimer to PABP1, and this interaction is conserved across different IAV strains. Unexpectedly, NS1 does not bind to PABP1 that is bound to poly(A) RNA. Instead, NS1 only binds to PABP1 free of RNA, suggesting that translation stimulation does not occur by NS1 interacting with the PABP1 molecule attached to the mRNA 3′-poly(A) tail. We propose that NS1 binds to the eIF4G complex at the 5′-end of the mRNA and recruits the RNA-free PABP1, which may stimulate translation initiation by promoting the association of the ribosomal subunits.

中文翻译:

甲型流感病毒NS1蛋白以二聚体的形式与无RNA的PABP1结合,但与PABP1-Poly(A)RNA复合体没有结合

甲型流感病毒(IAV)是一种高度传染性的人类病原体,每年造成近一百万人死亡。非结构蛋白1(NS1)是IAV表达的逃避宿主免疫系统的关键蛋白。另外,由于NS1具有结合poly(A)结合蛋白1(PABP1)和真核起始因子4G(eIF4G)的能力,因此已被提议刺激翻译。我们使用定量技术分析了NS1与PABP1的相互作用。我们的研究表明,NS1作为同二聚体与PABP1结合,并且这种相互作用在不同的IAV株之间是保守的。出乎意料的是,NS1不绑定到绑定到poly(A)RNA的PABP1。相反,NS1仅与不含RNA的PABP1结合,表明NS1与附着在mRNA 3'-poly(A)尾部的PABP1分子相互作用不会发生翻译刺激。
更新日期:2020-08-11
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