Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/70843
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dc.contributor.authorVijayapalani, P.en_US
dc.contributor.authorChen, J.C.F.en_US
dc.contributor.authorLiou, M.R.en_US
dc.contributor.authorChen, H.C.en_US
dc.contributor.authorHsu, Y.H.en_US
dc.contributor.authorLin, N.S.en_US
dc.date2012zh_TW
dc.date.accessioned2014-06-11T06:00:28Z-
dc.date.available2014-06-11T06:00:28Z-
dc.identifier.issn0305-1048zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/70843-
dc.description.abstractBamboo 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.en_US
dc.language.isoen_USzh_TW
dc.relationNucleic Acids Researchen_US
dc.relation.ispartofseriesNucleic Acids Research, Volume 40, Issue 2, Page(s) 638-649.en_US
dc.relation.urihttp://dx.doi.org/10.1093/nar/gkr705en_US
dc.subjectcell-to-cellen_US
dc.subjecttriple-gene-blocken_US
dc.subjectcucumber-necrosis-tombusvirusen_US
dc.subjectin-vitroen_US
dc.subjectphosphorylationen_US
dc.subjectviral movement proteinsen_US
dc.subjectgenome-linked proteinen_US
dc.subjectcapsiden_US
dc.subjectproteinen_US
dc.subjectcoat proteinen_US
dc.subjectsubcellular-localizationen_US
dc.subjectplasmodesmal transporten_US
dc.titlePhosphorylation of bamboo mosaic virus satellite RNA (satBaMV)-encoded protein P20 downregulates the formation of satBaMV-P20 ribonucleoprotein complexen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1093/nar/gkr705zh_TW
item.languageiso639-1en_US-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.openairetypeJournal Article-
item.fulltextno fulltext-
item.grantfulltextnone-
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