Key Laboratory of Biopesticide and Chemical Biology, Ministry of Education, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
College of Plant Protection, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Biomed Res Int. 2020 Jun 16;2020:5182164. doi: 10.1155/2020/5182164. eCollection 2020.
p2 of may translocate from the nucleus to the cytoplasm and recruit nucleolar functions to promote virus systemic movement. Cajal bodies (CBs) are nuclear components associated with the nucleolus, which play a major role in plant virus infection. Coilin, a marker protein of CBs, is essential for CB formation and function. Coilin contains three domains, the N-terminal, the center, and the C-terminal fragments. Using yeast two-hybrid, colocalization, and bimolecular fluorescence complementation (BiFC) approaches, we show that p2 interacts with the full-length of coilin (Atcoilin), the center and C-terminal domain of Atcoilin in the nucleus. Moreover, the N-terminal is indispensable for Atcoilin to interact with Cajal bodies.
p2 可能从核内易位到细胞质,并募集核仁功能以促进病毒的全身运动。Cajal 体(CBs)是与核仁相关的核内成分,在植物病毒感染中起主要作用。Cajal 体的标记蛋白 coilin 对于 CB 的形成和功能至关重要。coilin 包含三个结构域,即 N 端、中心和 C 端片段。利用酵母双杂交、共定位和双分子荧光互补(BiFC)方法,我们表明 p2 在核内与 coilin(Atcoilin)全长、Atcoilin 的中心和 C 端结构域相互作用。此外,N 端对于 Atcoilin 与 Cajal 体相互作用是必不可少的。