Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/50368
標題: Identification of the RNA-binding sites of the triple gene block protein 1 of bamboo mosaic potexvirus
作者: Wung, C.H.
徐堯煇
Hsu, Y.H.
Liou, D.Y.
Huang, W.C.
Lin, N.S.
Chang, B.Y.
關鍵字: virus movement protein
polymerase chain-reaction
stranded
nucleic-acids
to-cell transport
subcellular-localization
nucleotide-sequence
overlap extension
genomic rna
in-vitro
domain
期刊/報告no:: Journal of General Virology, Volume 80, Page(s) 1119-1126.
摘要: The triple gene block protein 1 (TGBp1) encoded by open reading frame 2 of bamboo mosaic potexvirus (BaMV) was overexpressed in Escherichia coli and purified in order to test its RNA-binding activity. UV crosslinking assays revealed that the RNA-binding activity was present mainly in the soluble fraction of the refolded TGBp1. The binding activity was nonspecific and salt concentration-dependent: activity was present at 0-50 mM NaCl but was almost abolished at 200 mM. The RNA-binding domain was located by deletion mutagenesis to the N-terminal 3-24 amino acids of TGBp1. Sequence alignment analysis of the N-terminal 25 amino acids of the TGBp1 homologues of potexviruses identified three arginine residues. Arg-to-Ala substitution at any one of the three arginines eliminated most of the RNA-binding activity, indicating that they were all critical to the RNA-binding activity of the TGBp1 of BaMV.
URI: http://hdl.handle.net/11455/50368
ISSN: 0022-1317
Appears in Collections:生物科技學研究所

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