Vidic Jasmina, Noiray Magali, Bagchi Angshuman, Slama-Schwok Anny
Paris Saclay University , UR892, INRA, 78350 Jouy en Josas, France.
UMS IPSIT-Intermol, University Paris Sud, Paris Saclay University , 92296 Châtenay-Malabry, France.
Biochemistry. 2016 Aug 9;55(31):4259-62. doi: 10.1021/acs.biochem.6b00514. Epub 2016 Jul 28.
The structure of the ribonucleoprotein complexes is crucial to viral transcription and replication of influenza virus, but association of the nucleoprotein (NP) with the polymerase remains to be characterized at the molecular level. Here, we identify a peptide of the polymerase acidic subunit PA(1-27) that associates with NP. Docking and molecular dynamics simulations suggest a similar NP binding site with PA(1-27) and PA(1-186). The PA(1-27)-NP complex is characterized by surface plasmon resonance and fluorescence using recombinant NP proteins and by pull-down assays in infected cells. The PA(1-27)-NP complex may have a role in the final steps of transcription and replication.
核糖核蛋白复合体的结构对于流感病毒的转录和复制至关重要,但核蛋白(NP)与聚合酶的关联在分子水平上仍有待表征。在此,我们鉴定出聚合酶酸性亚基PA(1 - 27)的一个与NP相关联的肽段。对接和分子动力学模拟表明PA(1 - 27)和PA(1 - 186)具有相似的NP结合位点。使用重组NP蛋白通过表面等离子体共振和荧光对PA(1 - 27)-NP复合体进行表征,并在受感染细胞中通过下拉试验进行表征。PA(1 - 27)-NP复合体可能在转录和复制的最后步骤中发挥作用。