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標題: | Phosphorylation of bamboo mosaic virus satellite RNA (satBaMV)-encoded protein P20 downregulates the formation of satBaMV-P20 ribonucleoprotein complex | 作者: | Vijayapalani, P. Chen, J.C.F. Liou, M.R. Chen, H.C. Hsu, Y.H. Lin, N.S. |
關鍵字: | cell-to-cell;triple-gene-block;cucumber-necrosis-tombusvirus;in-vitro;phosphorylation;viral movement proteins;genome-linked protein;capsid;protein;coat protein;subcellular-localization;plasmodesmal transport | Project: | Nucleic Acids Research | 期刊/報告no:: | Nucleic Acids Research, Volume 40, Issue 2, Page(s) 638-649. | 摘要: | Bamboo mosaic virus (BaMV) satellite RNA (satBaMV) depends on BaMV for its replication and encapsidation. SatBaMV-encoded P20 protein is an RNA-binding protein that facilitates satBaMV systemic movement in co-infected plants. Here, we examined phosphorylation of P20 and its regulatory functions. Recombinant P20 (rP20) was phosphorylated by host cellular kinase(s) in vitro, and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and mutational analyses revealed Ser-11 as the phosphorylation site. The phosphor-mimic rP20 protein interactions with satBaMV-translated mutant P20 were affected. In overlay assay, the Asp mutation at S11 (S11D) completely abolished the self-interaction of rP20 and significantly inhibited the interaction with both the WT and S11A rP20. In chemical cross-linking assays, S11D failed to oligomerize. Electrophoretic mobility shift assay and subsequent Hill transformation analysis revealed a low affinity of the phosphomimicking rP20 for satBaMV RNA. Substantial modulation of satBaMV RNA conformation upon interaction with nonphospho-mimic rP20 in circular dichroism analysis indicated formation of stable satBaMV ribonucleoprotein complexes. The dissimilar satBaMV translation regulation of the nonphosphoand phospho-mimic rP20 suggests that phosphorylation of P20 in the ribonucleoprotein complex converts the translation-incompetent satBaMV RNA to messenger RNA. The phospho-deficient or phospho-mimicking P20 mutant of satBaMV delayed the systemic spread of satBaMV in co-infected Nicotiana benthamiana with BaMV. Thus, satBaMV likely regulates the formation of satBaMV RNP complex during co-infection in planta. |
URI: | http://hdl.handle.net/11455/70843 | ISSN: | 0305-1048 | DOI: | 10.1093/nar/gkr705 |
Appears in Collections: | 期刊論文 |
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