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National Chung Hsing University Institutional Repository - NCHUIR > 農業暨自然資源學院 > 生物科技學研究所 > 依資料類型分類 > 期刊論文 >  Bamboo mosaic potexvirus satellite RNA (satBaMV RNA)-encoded P20 protein preferentially binds to satBaMV RNA

Please use this identifier to cite or link to this item: http://nchuir.lib.nchu.edu.tw/handle/309270000/131159

標題: Bamboo mosaic potexvirus satellite RNA (satBaMV RNA)-encoded P20 protein preferentially binds to satBaMV RNA
作者: Tsai, M.S.;Hsu, Y.H.;Lin, N.S.
徐堯煇
關鍵字: hepatitis-delta-virus;nucleic-acid;movement protein;coat protein;nucleotide-sequence;cooperative binding;encoded protein;replication;peptides;antigen
日期: 1999
Issue Date: 2012-12-07 16:18:33 (UTC+8)
關連: Journal of Virology, Volume 73, Issue 4, Page(s) 3032-3039.
摘要: A satellite RNA of 836 nucleotides [excluding the poly(A) tail] depends on the bamboo mosaic potexvirus (BaMV) for its replication and encapsidation. The BaMV satellite RNA (satBaMV) contains a single open reading frame encoding a 20-kDa nonstructural protein (P20). The P20 protein with eight histidine residues at the C terminus was overexpressed in Escherichia coli. Experiments of gel retardation, UV cross-linking, and Northwestern hybridization demonstrated that purified P20 was a nucleic-acid-binding protein. The binding of P20 to nucleic acids was strong and highly cooperative. P20 preferred binding to satBaMV- or BaMV-related sequences rather than to nonrelated sequences, By deletion analysis, the P20 binding sites were mainly located at the 5' and 3' untranslated regions of satBaMV RNA, and the RNA-protein interactions could compete with the poly(G) and, less efficiently, with the poly(U) homopolymers, The N-terminal arginine-rich motif of P20 was the RNA binding domain, as shown by in-frame deletion analysis. This is the first report that a plant virus satellite RNA-encoded nonstructural protein preferentially binds with nucleic acids.
Relation: Journal of Virology
Appears in Collections:[依資料類型分類] 期刊論文
[依教師分類] 徐堯煇

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