ArticleJournal of molecular biology2010
The macroscopic rate of nucleic acid translocation by hepatitis C virus helicase NS3h is dependent on both sugar and base moieties.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Characterization of a multipurpose NS3 surface patch coordinating HCV replicase assembly and virion morphogenesis.PLoS pathogens · 2022Article
- The Role of XPB/Ssl2 dsDNA Translocase Processivity in Transcription Start-site Scanning.Journal of molecular biology · 2021Article
- Remodeler Catalyzed Nucleosome Repositioning: Influence of Structure and Stability.International journal of molecular sciences · 2020Review
- Single-molecule fluorescence imaging: Generating insights into molecular interactions in virology.Journal of biosciences · 2018Review
- Modulation of Escherichia coli UvrD Single-Stranded DNA Translocation by DNA Base Composition.Biophysical journal · 2017Article
- Single-molecule imaging reveals the translocation and DNA looping dynamics of hepatitis C virus NS3 helicase.Protein science : a publication of the Protein Society · 2017Article
- Computational study of remodeling in a nucleosomal array.The European physical journal. E, Soft matter · 2015Article
- 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
- Double-stranded DNA translocase activity of transcription factor TFIIH and the mechanism of RNA polymerase II open complex formation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Monomeric nature of dengue virus NS3 helicase and thermodynamic analysis of the interaction with single-stranded RNA.Nucleic acids research · 2014Article
- Quantitative determination of binding of ISWI to nucleosomes and DNA shows allosteric regulation of DNA binding by nucleotides.Biochemistry · 2014Article
- ISWI remodels nucleosomes through a random walk.Biochemistry · 2014Article
- Kinetic mechanism of DNA translocation by the RSC molecular motor.Archives of biochemistry and biophysics · 2013Article
- Article
- Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis.Journal of molecular biology · 2012Article
- Allosteric interactions of DNA and nucleotides with S. cerevisiae RSC.Biochemistry · 2011Article
- Unmasking the active helicase conformation of nonstructural protein 3 from hepatitis C virus.Journal of virology · 2011Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The nonstructural protein 3 helicase (NS3h) of hepatitis C virus is a 3'-to-5' superfamily 2 RNA and DNA helicase that is essential for the replication of hepatitis C virus. We have examined the kinetic mechanism of the translocation of NS3h along single-stranded nucleic acid with bases uridylate (rU), deoxyuridylate (dU), and deoxythymidylate (dT), and have found that the macroscopic rate of translocation is dependent on both the base moiety and the sugar moiety of the nucleic acid, with approximate macroscopic translocation rates of 3 nt s(-1) (oligo(dT)), 35 nt s(-1) (oligo(dU)), and 42 nt s(-1) (oligo(rU)), respectively. We found a strong correlation between the macroscopic translocation rates and the binding affinity of the translocating NS3h protein for the respective substrates such that weaker affinity corresponded to faster translocation. The values of K(0.5) for NS3h translocation at a saturating ATP concentration are as follows: 3.3+/-0.4 microM nucleotide (poly(dT)), 27+/-2 microM nucleotide (poly(dU)), and 36+/-2 microM nucleotide (poly(rU)). Furthermore, results of the isothermal titration of NS3h with these oligonucleotides suggest that differences in TDeltaS(0) are the principal source of differences in the affinity of NS3h binding to these substrates. Interestingly, despite the differences in macroscopic translocation rates and binding affinities, the ATP coupling stoichiometries for NS3h translocation were identical for all three substrates (approximately 0.5 ATP molecule consumed per nucleotide translocated). This similar periodicity of ATP consumption implies a similar mechanism for NS3h translocation along RNA and DNA substrates.
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