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Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein
- Source :
-
FEBS Letters . Feb2009, Vol. 583 Issue 4, p691-696. 6p. - Publication Year :
- 2009
-
Abstract
- 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. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 583
- Issue :
- 4
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 36566495
- Full Text :
- https://doi.org/10.1016/j.febslet.2009.01.008