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

Chun Chung Wang, Zhi Shun Huang, Pei Ling Chiang, Chien Tsun Chen, Huey Nan Wu

Research output: Contribution to journalArticle

38 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)691-696
Number of pages6
JournalFEBS Letters
Volume583
Issue number4
DOIs
Publication statusPublished - Feb 18 2009

Fingerprint

Nucleoside-Triphosphatase
RNA
Viral RNA
DNA
Divalent Cations
Ionic strength
Osmolar Concentration
Adenosine Triphosphatases
RNA triphosphatase
flavivirus NS3 protein
Substrates

Keywords

  • Dengue virus
  • NS3 helicase
  • NTPase activity
  • RTPase activity
  • Unwinding activity

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein. / Wang, Chun Chung; Huang, Zhi Shun; Chiang, Pei Ling; Chen, Chien Tsun; Wu, Huey Nan.

In: FEBS Letters, Vol. 583, No. 4, 18.02.2009, p. 691-696.

Research output: Contribution to journalArticle

Wang, Chun Chung ; Huang, Zhi Shun ; Chiang, Pei Ling ; Chen, Chien Tsun ; Wu, Huey Nan. / Analysis of the nucleoside triphosphatase, RNA triphosphatase, and unwinding activities of the helicase domain of dengue virus NS3 protein. In: FEBS Letters. 2009 ; Vol. 583, No. 4. pp. 691-696.
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