Model-based structural and functional characterization of the Rice stripe tenuivirus nucleocapsid protein interacting with viral genomic RNA
文献类型: 外文期刊
作者: Lu, Gang 1 ; Li, Jia 1 ; Zhou, Yijun 2 ; Zhou, Xueping 3 ; Tao, Xiaorong 1 ;
作者机构: 1.Nanjing Agr Univ, Dept Plant Pathol, Nanjing 210095, Jiangsu, Peoples R China
2.Jiangsu Acad Agr Sci, Inst Plant Protect, Nanjing 210014, Jiangsu, Peoples R China
3.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol, Hangzhou 310029, Zhejiang, Peoples R China
4.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing, Peoples R China
关键词: Model-based structure-function analysis;Rice Stripe Tenuivirus;Nucleocapsid Protein;RNA-binding sites
期刊名称:VIROLOGY ( 影响因子:3.616; 五年影响因子:3.967 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: Rice stripe tenuivirus (RSV) is a filamentous, negative-strand RNA virus causing severe diseases on rice in Asian countries. The viral particle is composed predominantly of a nucleocapsid protein (NP) and genomic RNA. However, the molecular details of how the RSV NP interacts with genomic RNA during particle assembly remain largely unknown. Here, we modeled the NP-RNA complex and show that polar amino acids within a predicted groove of NP are critical for RNA binding and protecting the RNA from RNase digestion. RSV NP formed pentamers, hexamers, heptamers, and octamers. By modeling the higher-order structures, we found that oligomer formation was driven by the N-terminal amino arm of the NP. Deletion of this arm abolished oligomerization; the N-terminally truncated NP was less able to interact with RNA and protect RNA than was the wild type. These findings afford valuable new insights into molecular mechanism of RSV NPs interacting with genomic RNA.
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