中文摘要：水稻条纹病毒（RSV）P3蛋白是植物RNA沉默抑制子。通过生物分子荧光互补技术已经证明P3参与了植物的自相互作用，但是负责同型相互作用的区域尚未确定。本研究利用酵母双杂交、免疫共沉淀和荧光实验分析了P3自相互作用的结构域。结果表明：P3在酵母和昆虫细胞中也能与自身进行相互作用。负责P3- P3交互作用的结构域映射到P3 N末端第15个到第30个氨基酸。此外，亚细胞定位表明：同源寡聚是P3在昆虫细胞核内形成较大蛋白质聚集体的先决条件。
外文摘要：Rice stripe virus (RSV) protein P3 is a suppressor of RNA silencing in plants. P3 has been shown by biomolecular fluorescence complementation assay to self-interact in planta but the regions responsible for homotypic interaction have not been determined. Here we analyzed the domains for the self-interaction of P3 by using yeast two-hybrid, co-immunoprecipitation and fluorescence experiments. The results showed that P3 was also able to interact with itself in yeast and insect cells. The domain responsible for P3-P3 interaction was mapped to amino acids 15-30 at the N-terminal region of P3. Furthermore, subcellular localization suggested that the homo-oligomerization was the prerequisite for P3 to form larger protein aggregates in the nucleus of insect cell.
外文关键词：rice stripe virus; P3; self-interaction; yeast two-hybrid; co-immunoprecipitation
作者：Zhao, S. L.; Hao, J. H.; Xue, Y. N.; 等
作者单位：扬州大学
期刊名称：ACTA VIROLOGICA
期刊影响因子：7.003
出版年份：2016
出版刊次：3
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