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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Acid Anhydride Hydrolases / genetics
-
Acid Anhydride Hydrolases / metabolism*
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Cloning, Molecular
-
Dengue Virus / genetics
-
Dengue Virus / metabolism*
-
Escherichia coli / genetics
-
Histidine / chemistry
-
Molecular Sequence Data
-
Mutation
-
Nucleoside-Triphosphatase / genetics
-
Nucleoside-Triphosphatase / metabolism*
-
Protein Structure, Tertiary
-
RNA Helicases / chemistry
-
RNA Helicases / classification
-
RNA Helicases / genetics
-
RNA Helicases / metabolism
-
Recombinant Proteins / isolation & purification
-
Recombinant Proteins / metabolism
-
Serine Endopeptidases / chemistry
-
Serine Endopeptidases / classification
-
Serine Endopeptidases / genetics
-
Serine Endopeptidases / metabolism
-
Serotyping
-
Viral Nonstructural Proteins / chemistry*
-
Viral Nonstructural Proteins / classification
-
Viral Nonstructural Proteins / genetics
-
Viral Nonstructural Proteins / metabolism*
Substances
-
NS3 protein, flavivirus
-
Recombinant Proteins
-
Viral Nonstructural Proteins
-
Histidine
-
Serine Endopeptidases
-
Acid Anhydride Hydrolases
-
RNA triphosphatase
-
Nucleoside-Triphosphatase
-
RNA Helicases