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FEBS Lett. 2009 Feb 18;583(4):691-6. doi: 10.1016/j.febslet.2009.01.008. Epub 2009 Jan 21.

Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein.

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1
Institute of Molecular Biology, Academia Sinica, Nankang, 115 Taipei, Taiwan.

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.

PMID:
19166847
DOI:
10.1016/j.febslet.2009.01.008
[Indexed for MEDLINE]
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