摘要
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.
原文 | 英語 |
---|---|
頁(從 - 到) | 691-696 |
頁數 | 6 |
期刊 | FEBS Letters |
卷 | 583 |
發行號 | 4 |
DOIs | |
出版狀態 | 已發佈 - 二月 18 2009 |
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology