ArticleThe Journal of biological chemistry2008
Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
- Positive strand RNA viruses differ in the constraints they place on the folding of their negative strand.RNA (New York, N.Y.) · 2022Article
- Monitoring helicase-catalyzed unwinding of multiple duplexes simultaneously.Methods in enzymology · 2022Article
- Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights fromInternational journal of molecular sciences · 2021Review
- DNA-Unwinding Dynamics of Escherichia coli UvrD Lacking the C-Terminal 40 Amino Acids.Biophysical journal · 2020Article
- Zika virus NS3 is a canonical RNA helicase stimulated by NS5 RNA polymerase.Nucleic acids research · 2019Article
- Quantitative microspectroscopic imaging reveals viral and cellular RNA helicase interactions in live cells.The Journal of biological chemistry · 2017Article
- ATP dependent NS3 helicase interaction with RNA: insights from molecular simulations.Nucleic acids research · 2015Article
- Monomeric nature of dengue virus NS3 helicase and thermodynamic analysis of the interaction with single-stranded RNA.Nucleic acids research · 2014Article
- Aurintricarboxylic acid modulates the affinity of hepatitis C virus NS3 helicase for both nucleic acid and ATP.Biochemistry · 2013Article
- Discovering new medicines targeting helicases: challenges and recent progress.Journal of biomolecular screening · 2013Review
- Translocation of Saccharomyces cerevisiae Pif1 helicase monomers on single-stranded DNA.Nucleic acids research · 2013Article
- Single-molecule imaging of the oligomer formation of the nonhexameric Escherichia coli UvrD helicase.Biophysical journal · 2013Article
- Structure and Mechanisms of SF1 DNA Helicases.Advances in experimental medicine and biology · 2013Article
- Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA.Biochemistry · 2012Article
- Article
- The acidic sequence of the NS4A cofactor regulates ATP hydrolysis by the HCV NS3 helicase.Archives of virology · 2011Article
- Double-stranded RNA-dependent ATPase DRH-3: insight into its role in RNAsilencing in Caenorhabditis elegans.The Journal of biological chemistry · 2010Article
- Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral target.The Journal of biological chemistry · 2010Review
- Investigation of translocation, DNA unwinding, and protein displacement by NS3h, the helicase domain from the hepatitis C virus helicase.Biochemistry · 2010Article
- Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
HCV NS3 helicase exhibits activity toward DNA and RNA substrates. The DNA helicase activity of NS3 has been proposed to be optimal when multiple NS3 molecules are bound to the same substrate molecule. NS3 catalyzes little or no measurable DNA unwinding under single cycle conditions in which the concentration of substrate exceeds the concentration of enzyme by 5-fold. However, when NS3 (100 nm) is equimolar with the substrate, a small burst amplitude of approximately 8 nm is observed. The burst amplitude increases as the enzyme concentration increases, consistent with the idea that multiple molecules are needed for optimal unwinding. Protein-protein interactions may facilitate optimal activity, so the oligomeric properties of the enzyme were investigated. Chemical cross-linking indicates that full-length NS3 forms higher order oligomers much more readily than the NS3 helicase domain. Dynamic light scattering indicates that full-length NS3 exists as an oligomer, whereas NS3 helicase domain exists in a monomeric form in solution. Size exclusion chromatography also indicates that full-length NS3 behaves as an oligomer in solution, whereas the NS3 helicase domain behaves as a monomer. When NS3 was passed through a small pore filter capable of removing protein aggregates, greater than 95% of the protein and the DNA unwinding activity was removed from solution. In contrast, only approximately 10% of NS3 helicase domain and approximately 20% of the associated DNA unwinding activity was removed from solution after passage through the small pore filter. The results indicate that the optimally active form of full-length NS3 is part of an oligomeric species in vitro.
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