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A non-structural protein encoded by Rice Dwarf Virus targets to the nucleus and chloroplast and inhibits local RNA silencing
Authors:Gao  Feng  Zhao  Shanshan  Men  Shuzhen  Kang  Zhensheng  Hong  Jian  Wei  Chunhong  Hong  Wei  Li  Yi
Institution:1.The State Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, 100871, China
;2.Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland, 20742, USA
;3.College of Plant Protection, Fujian Agriculture & Forestry University, Fuzhou, 350002, China
;4.College of Life Sciences, Nankai University, Tianjin, 300071, China
;5.Department of Plant Protection, Northwestern Agriculture and Forestry University, Yangling, 712100, China
;6.College of Agriculture, Zhejiang University, Hangzhou, 310029, China
;7.The First Affiliated Hospital of Zhejiang Chinese Medical University, Hangzhou, 310006, China
;
Abstract:

RNA silencing is a potent antiviral mechanism in plants and animals. As a counter-defense, many viruses studied to date encode one or more viral suppressors of RNA silencing (VSR). In the latter case, how different VSRs encoded by a virus function in silencing remains to be fully understood. We previously showed that the nonstructural protein Pns10 of a Phytoreovirus, Rice dwarf virus (RDV), functions as a VSR. Here we present evidence that another nonstructural protein, Pns11, also functions as a VSR. While Pns10 was localized in the cytoplasm, Pns11 was localized both in the nucleus and chloroplasts. Pns11 has two bipartite nuclear localization signals (NLSs), which were required for nuclear as well as chloroplastic localization. The NLSs were also required for the silencing activities of Pns11. This is the first report that multiple VSRs encoded by a virus are localized in different subcellular compartments, and that a viral protein can be targeted to both the nucleus and chloroplast. These findings may have broad significance in studying the subcellular targeting of VSRs and other viral proteins in viral-host interactions.

Keywords:
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