Movement Protein Pns6 of Rice dwarf phytoreovirus Has Both ATPase and RNA Binding Activities
文献类型: 外文期刊
作者: Ji, Xu 1 ; Qian, Dan 1 ; Wei, Chunhong 1 ; Ye, Gongyin 2 ; Zhang, Zhongkai 3 ; Wu, Zujian 4 ; Xie, Lianhui 4 ; Li, Yi 1 ;
作者机构: 1.Peking Univ, State Key Lab Prot & Plant Gene Res, Peking Yale Joint Ctr Plant Mol Genet & Agrobiote, Coll Life Sci, Beijing 100871, Peoples R China
2.Zhejiang Univ, State Key Lab Rice Biol, Inst Insect Sci, Hangzhou 310003, Zhejiang, Peoples R China
3.Yunnan Acad Agr Sci, Biotechnol & Genet Resources Inst, Kunming, Peoples R China
4.Fujian Agr & Forestry Univ, Key Lab Plant Virol Fujian Prov, Inst Plant Virol, Fuzhou, Peoples R China
期刊名称:PLOS ONE ( 影响因子:3.24; 五年影响因子:3.788 )
ISSN: 1932-6203
年卷期: 2011 年 6 卷 9 期
页码:
收录情况: SCI
摘要: Cell-to-cell movement is essential for plant viruses to systemically infect host plants. Plant viruses encode movement proteins (MP) to facilitate such movement. Unlike the well-characterized MPs of DNA viruses and single-stranded RNA (ssRNA) viruses, knowledge of the functional mechanisms of MPs encoded by double-stranded RNA (dsRNA) viruses is very limited. In particular, many studied MPs of DNA and ssRNA viruses bind non-specifically ssRNAs, leading to models in which ribonucleoprotein complexes (RNPs) move from cell to cell. Thus, it will be of special interest to determine whether MPs of dsRNA viruses interact with genomic dsRNAs or their derivative sRNAs. To this end, we studied the biochemical functions of MP Pns6 of Rice dwarf phytoreovirus (RDV), a member of Phytoreovirus that contains a 12-segmented dsRNA genome. We report here that Pns6 binds both dsRNAs and ssRNAs. Intriguingly, Pns6 exhibits non-sequence specificity for dsRNA but shows preference for ssRNA sequences derived from the conserved genomic 5'- and 3'-terminal consensus sequences of RDV. Furthermore, Pns6 exhibits magnesium-dependent ATPase activities. Mutagenesis identified the RNA binding and ATPase activity sites of Pns6 at the N- and C-termini, respectively. Our results uncovered the novel property of a viral MP in differentially recognizing dsRNA and ssRNA and establish a biochemical basis to enable further studies on the mechanisms of dsRNA viral MP functions.
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