ArticleThe Journal of biological chemistry2003
Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action.
Article in The Journal of biological chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 61 citations in OpenAlex.
- Hepatitis C virus NS3 helicase contributes to (-) strand RNA synthesis.Nature communications · 2025Article
- Analogs of NIH Molecular Probe ML283 Are Potent SARS-CoV-2 Helicase Inhibitors.ACS chemical biology · 2025Article
- From viruses to cancer: exploring the role of the hepatitis C virus NS3 protein in carcinogenesis.Infectious agents and cancer · 2024Review
- Conserved motifs in the flavivirus NS3 RNA helicase enzyme.Wiley interdisciplinary reviews. RNA · 2022Review
- Dissection of two drug-targeted regions of Hepatitis C virus subtype 4a infecting Egyptian patients.Virus genes · 2020Article
- Molecular determinants for dsDNA translocation by the transcription-repair coupling and evolvability factor Mfd.Nature communications · 2020Article
- Motif V regulates energy transduction between the flavivirus NS3 ATPase and RNA-binding cleft.The Journal of biological chemistry · 2020Article
- Function of a strand-separation pin element in the PriA DNA replication restart helicase.The Journal of biological chemistry · 2019Article
- Allostery in the dengue virus NS3 helicase: Insights into the NTPase cycle from molecular simulations.PLoS computational biology · 2018Article
- NS3 from Hepatitis C Virus Strain JFH-1 Is an Unusually Robust Helicase That Is Primed To Bind and Unwind Viral RNA.Journal of virology · 2018Article
- Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.RNA (New York, N.Y.) · 2017Article
- Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction.Biochemistry · 2015Article
- X-ray structure of the pestivirus NS3 helicase and its conformation in solution.Journal of virology · 2015Article
- Grip it and rip it: structural mechanisms of DNA helicase substrate binding and unwinding.Protein science : a publication of the Protein Society · 2014Review
- pH-dependent conformational changes in the HCV NS3 protein modulate its ATPase and helicase activities.PloS one · 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
- Primuline derivatives that mimic RNA to stimulate hepatitis C virus NS3 helicase-catalyzed ATP hydrolysis.The Journal of biological chemistry · 2013Article
- Structure and Mechanisms of SF1 DNA Helicases.Advances in experimental medicine and biology · 2013Article
- Significance of monoclonal antibodies against the conserved epitopes within non-structural protein 3 helicase of hepatitis C virus.PloS one · 2013Article
- The T4 phage SF1B helicase Dda is structurally optimized to perform DNA strand separation.Structure (London, England : 1993) · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The hepatitis C virus (HCV) NS3 helicase shares several conserved motifs with other superfamily 2 (SF2) helicases. Besides these sequences, several additional helicase motifs are conserved among the various HCV genotypes and quasispecies. The roles of two such motifs are examined here. The first motif (YRGXDV) forms a loop that connects SF2 helicase motifs 4 and 5, at the tip of which is Arg393. When Arg393 is changed to Ala, the resulting protein (R393A) retains a nucleic acid stimulated ATPase but cannot unwind RNA. R393A also unwinds DNA more slowly than wild type and translocates poorly on single-stranded DNA (ssDNA). DNA and RNA stimulate ATP hydrolysis catalyzed by R393A like the wild type, but the mutant protein binds ssDNA more weakly both in the presence and absence of the non-hydrolyzable ATP analog ADP(BeF3). The second motif (DFSLDPTF) forms a loop that connects two anti-parallel sheets between SF2 motifs 5 and 6. When Phe444 in this Phe-loop is changed to Ala, the resulting protein (F444A) is devoid of all activities. When Phe438 is changed to Ala, the protein (F438A) retains nucleic acid-stimulated ATPase, but does not unwind RNA. F438A unwinds DNA and translocates on ssDNA at about half the rate of the wild type. Equilibrium binding data reveal that this uncoupling of ATP hydrolysis and unwinding is due to the fact that the F438A mutant does not release ssDNA upon ATP binding like the wild type. A model is presented explaining the roles of the Arg-clamp and the Phe-loop in the unwinding reaction.
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