ArticleThe Journal of biological chemistry2009
NS3 helicase from the hepatitis C virus can function as a monomer or oligomer depending on enzyme and substrate concentrations.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 42 citations in OpenAlex.
- NS5 polymerase stimulates RNA duplex unwinding by the Orthoflavivirus NS3 helicase.The Journal of biological chemistry · 2026Article
- Unwinding of an RNA duplex by the Orthoflavivirus NS3 helicase requires translocation beyond the displaced strand and is stimulated by the NS5 RdRp.bioRxiv : the preprint server for biology · 2026Article
- 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
- Zika virus NS3 is a canonical RNA helicase stimulated by NS5 RNA polymerase.Nucleic acids research · 2019Article
- Structure and function of Pif1 helicase.Biochemical Society transactions · 2017Review
- Quantitative microspectroscopic imaging reveals viral and cellular RNA helicase interactions in live cells.The Journal of biological chemistry · 2017Article
- Protein-protein interaction analysis for functional characterization of helicases.Methods (San Diego, Calif.) · 2016Review
- ATP dependent NS3 helicase interaction with RNA: insights from molecular simulations.Nucleic acids research · 2015Article
- Mechanisms of HCV NS3 helicase monitored by optical tweezers.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Yeast Pif1 accelerates annealing of complementary DNA strands.Biochemistry · 2014Article
- Hepatitis C virus RNA replication and virus particle assembly require specific dimerization of the NS4A protein transmembrane domain.Journal of virology · 2014Article
- The interdomain interface in bifunctional enzyme protein 3/4A (NS3/4A) regulates protease and helicase activities.Protein science : a publication of the Protein Society · 2013Article
- Aurintricarboxylic acid modulates the affinity of hepatitis C virus NS3 helicase for both nucleic acid and ATP.Biochemistry · 2013Article
- Translocation of Saccharomyces cerevisiae Pif1 helicase monomers on single-stranded DNA.Nucleic acids research · 2013Article
- Physical and functional interaction between yeast Pif1 helicase and Rim1 single-stranded DNA binding protein.Nucleic acids research · 2013Article
- Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA.Biochemistry · 2012Article
- Unwinding initiation by the viral RNA helicase NPH-II.Journal of molecular biology · 2012Article
- Single-base pair unwinding and asynchronous RNA release by the hepatitis C virus NS3 helicase.Science (New York, N.Y.) · 2011Article
- Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Hepatitis C virus NS3 helicase can unwind double-stranded DNA and RNA and has been proposed to form oligomeric structures. Here we examine the DNA unwinding activity of monomeric NS3. Oligomerization was measured by preparing a fluorescently labeled form of NS3, which was titrated with unlabeled NS3, resulting in a hyperbolic increase in fluorescence anisotropy and providing an apparent equilibrium dissociation constant of 236 nm. To evaluate the DNA binding activity of individual subunits within NS3 oligomers, two oligonucleotides were labeled with fluorescent donor or acceptor molecules and then titrated with NS3. Upon the addition of increasing concentrations of NS3, fluorescence energy transfer was observed, which reached a plateau at a 1:1 ratio of NS3 to oligonucleotides, indicating that each subunit within the oligomeric form of NS3 binds to DNA. DNA unwinding was measured under multiple turnover conditions with increasing concentrations of NS3; however, no increase in specific activity was observed, even at enzyme concentrations greater than the apparent dissociation constant for oligomerization. An ATPase-deficient form of NS3, NS3(D290A), was prepared to explore the functional consequences of oligomerization. Under single turnover conditions in the presence of excess concentration of NS3 relative to DNA, NS3(D290A) exhibited a dominant negative effect. However, under multiple turnover conditions in which DNA concentration was in excess to enzyme concentration, NS3(D290A) did not exhibit a dominant negative effect. Taken together, these data support a model in which monomeric forms of NS3 are active. Oligomerization of NS3 occurs, but subunits can function independently or cooperatively, dependent upon the relative concentration of the DNA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.