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    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/27762


    Title: Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein
    Authors: Wang,CC;Huang,ZS;Chiang,PL;Chen,CT;Wu,HN
    Contributors: 生命科學研究所
    Keywords: CRYSTAL-STRUCTURE;REPLICATION;POLYMERASE;MODULATION;INSIGHTS
    Date: 2009
    Issue Date: 2010-06-29 19:29:02 (UTC+8)
    Publisher: 中央大學
    Abstract: The helicase domain of dengue virus NS3 protein (DENV NS3H) contains RNA-stimulated nucleoside triphosphatase ( NTPase), ATPase/helicase, and RNA 5'-triphosphatase (RTPase) activities that are essential for viral RNA replication and capping. Here, we show that DENV NS3H unwinds 3'-tailed duplex with an RNA but not a DNA loading strand, and the helicase activity is poorly processive. The substrate of the divalent cation-dependent RTPase activity is not restricted to viral RNA 5'-terminus, a protruding 5'-terminus made the RNA 5'-triphosphate readily accessible to DENV NS3H. DENV NS3H preferentially binds RNA to DNA, and the functional interaction with RNA is sensitive to ionic strength. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
    Relation: FEBS LETTERS
    Appears in Collections:[生命科學研究所 ] 期刊論文

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