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作 者:苗淑月 叶倩 张宇 赵星月 王鑫 卢冰心 史晓斌[2] 张志代 郑立敏[2] 陈建斌[2] MIAO Shuyue;YE Qian;ZHANG Yu;ZHAO Xingyue;WANG Xin;LU Bingxin;SHI Xiaobin;ZHANG Zhidai;ZHENG Limin;CHEN Jianbin(Tobacco Research Institute,Henan Academy of Agricultural Sciences,Xuchang,Henan 461000,China;Institute of Plant Protection,Hunan Academy of Agricultural Sciences,Changsha,Hunan 410125,China;College of Horticulture and Plant Protection,Inner Mongolia Agricultural University,Hohhot,Inner Mongolia 010008,China;Agricultural and Rural Bureau of Mayang County,Mayang,Hunan 419400,China)
机构地区:[1]河南省农业科学院烟草研究所,河南许昌461000 [2]湖南省农业科学院植物保护研究所,湖南长沙410125 [3]内蒙古农业大学园艺与植物保护学院,内蒙古呼和浩特010008 [4]麻阳苗族自治县农业农村局,湖南麻阳419400
出 处:《作物研究》2023年第4期415-421,共7页Crop Research
基 金:国家重点研发计划政府间/港澳台重点专项(2018YFE0112600);国家自然科学基金(31871935);长沙市杰出创新青年培养计划(kq2009006);长沙市自然科学基金(kq2208140);湖南省农业科学院科技创新项目(2022CX105)。
摘 要:为了探究番茄斑萎病毒核衣壳蛋白N在马铃薯上的致病性,采用酵母双杂交和双分子荧光互补技术研究了病毒N蛋白的自身互作及其关键功能域。通过RT-PCR扩增了N基因全长及其截断突变体,并构建了酵母表达载体对其自身互作的功能区域进行鉴定。结果显示,在酵母细胞中N蛋白自身互作的关键功能域位于186位至193位氨基酸之间,且N蛋白在植物体内的互作主要发生在细胞核和细胞质中。研究结果可为番茄斑萎病毒的防控提供理论依据。In order to explore the pathogenicity of nucleocapsid protein N of tomato spotted wilt virus in potato,the self-interaction and key functional domains of viral N protein were studied by yeast two-hybrid and bimolecular fluorescence complementation techniques.The full-length N gene and its truncated mutants were amplified by RT-PCR,and yeast expre-ssion vectors were constructed to identify the functional regions interacting with themselves.The results showed that the key functional domain of N protein self-interaction in yeast cells was located between amino acid 186 and amino acid 193,and the interaction of N protein in plants mainly occurred in the nucleus and cytoplasm.The research results can provide a theoretical basis for the prevention and control of the outbreak of tomato spotted wilt virus.
分 类 号:S432.1[农业科学—植物病理学]
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