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Viroplasm Protein P9-1 of Rice Black-Streaked Dwarf Virus Preferentially Binds to Single-Stranded RNA in Its Octamer Form, and the Central Interior Structure Formed by This Octamer Constitutes the Major RNA Binding Site

文献类型： 外文期刊

作者： Wu, Jianyan 1 ; Li, Jia 1 ; Mao, Xiang 2 ; Wang, Weiwu 3 ; Cheng, Zhaobang 4 ; Zhou, Yijun 4 ; Zhou, Xueping 5 ; Tao, Xia 1 ;

作者机构： 1.Nanjing Agr Univ, Dept Plant Pathol, Minist Educ, Key Lab Integrated Management Crop Dis & Pests, Nanjing, Jiangsu, Peoples R China

2.Nanjing Agr Univ, Coll Vet Med, Nanjing, Jiangsu, Peoples R China

3.Nanjing Agr Univ, Coll Life Sci, Nanjing, Jiangsu, Peoples R China

4.Jiangsu Acad Agr Sci, Inst Plant Protect, Nanjing, Jiangsu, Peoples R China

5.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol, Hangzhou 310003, Zhejiang, Peoples R China

6.Chinese Acad Agr Sci, State Key Lab Biol Plant Dis & Insect Pests, Inst Plant Protect, Beijing 100193, Peoples R China

期刊名称：JOURNAL OF VIROLOGY （ 影响因子：5.103； 五年影响因子：5.078 ）

ISSN： 0022-538X

年卷期： 2013 年 87 卷 23 期

页码：

收录情况： SCI

摘要： The P9-1 protein of Rice black-streaked dwarf virus (RBSDV) is an essential part of the viroplasm. However, little is known about its nature or biological function in the viroplasm. In this study, the structure and function of P9-1 were analyzed for in vitro binding to nucleic acids. We found that the P9-1 protein preferentially bound to single-stranded versus double-stranded nucleic acids; however, the protein displayed no preference for RBSDV versus non-RBSDV single-stranded ssRNA (ssRNA). A gel mobility shift assay revealed that the RNA gradually shifted as increasing amounts of P9-1 were added, suggesting that multiple subunits of P9-1 bind to ssRNA. By using discontinuous blue native gel and chromatography analysis, we found that the P9-1 protein was capable of forming dimers, tetramers, and octamers. Strikingly, we demonstrated that P9-1 preferentially bound to ssRNA in the octamer, rather than the dimer, form. Deletion of the C-terminal arm resulted in P9-1 no longer forming octamers; consequently, the deletion mutant protein bound to ssRNA with significantly lower affinity and with fewer copies bound per ssRNA. Alanine substitution analysis revealed that electropositive amino acids among residues 25 to 44 are important for RNA binding and map to the central interior structure that was formed only by P9-1 octamers. Collectively, our findings provide novel insights into the structure and function of RBSDV viroplasm protein P9-1 binding to RNA.

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