Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/50385
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dc.contributor.authorCheng, C.W.en_US
dc.contributor.author徐堯煇zh_TW
dc.contributor.authorHsiao, Y.Y.en_US
dc.contributor.authorWu, H.C.en_US
dc.contributor.authorChuang, C.M.en_US
dc.contributor.authorChen, J.S.en_US
dc.contributor.authorTsai, C.H.en_US
dc.contributor.authorHsu, Y.H.en_US
dc.contributor.authorWu, Y.C.en_US
dc.contributor.authorLee, C.C.en_US
dc.contributor.authorMeng, M.S.A.en_US
dc.contributor.author孟孟孝zh_TW
dc.date2009zh_TW
dc.date.accessioned2014-06-06T08:49:25Z-
dc.date.available2014-06-06T08:49:25Z-
dc.identifier.issn0022-538Xzh_TW
dc.identifier.urihttp://hdl.handle.net/11455/50385-
dc.description.abstractBamboo mosaic virus (BaMV) is a 6.4-kb positive-sense RNA virus belonging to the genus Potexvirus of the family Flexiviridae. The 155-kDa viral replicase, the product of ORF1, comprises an N-terminal S-adenosyl-L-methionine (AdoMet)-dependent guanylyltransferase, a nucleoside triphosphatase/RNA 5'-triphosphatase, and a C-terminal RNA-dependent RNA polymerase (RdRp). To search for cellular factors potentially involved in the regulation of replication and/or transcription of BaMV, the viral RdRp domain was targeted as bait to screen against a leaf cDNA library of Nicotiana benthamiana using a yeast two-hybrid system. A putative methyltransferase (PNbMTS1) of 617 amino acid residues without an established physiological function was identified. Cotransfection of N. benthamiana protoplasts with a BaMV infectious clone and the PNbMTS1-expressing plasmid showed a PNbMTS1 dosage-dependent inhibitory effect on the accumulation of BaMV coat protein. Deletion of the N-terminal 36 amino acids, deletion of a predicted signal peptide or transmembrane segment, or mutations in the putative AdoMet-binding motifs of PNbMTS1 abolished the inhibitory effect. In contrast, suppression of PNbMTS1 by virus-induced gene silencing in N. benthamiana increased accumulation of the viral coat protein as well as the viral genomic RNA. Collectively, PNbMTS1 may function as an innate defense protein against the accumulation of BaMV through an uncharacterized mechanism.en_US
dc.language.isoen_USzh_TW
dc.relationJournal of Virologyen_US
dc.relation.ispartofseriesJournal of Virology, Volume 83, Issue 11, Page(s) 5796-5805.en_US
dc.relation.urihttp://dx.doi.org/10.1128/jvi.02471-08en_US
dc.subjectdependent rna-polymeraseen_US
dc.subjectgenes affecting replicationen_US
dc.subjects-adenosylmethionineen_US
dc.subjectarginine methylationen_US
dc.subjectgenomic rnaen_US
dc.subject1a proteinen_US
dc.subjectidentificationen_US
dc.subjectarabidopsisen_US
dc.subjectregionen_US
dc.subjectpotexvirusen_US
dc.titleSuppression of Bamboo Mosaic Virus Accumulation by a Putative Methyltransferase in Nicotiana benthamianaen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1128/jvi.02471-08zh_TW
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