ArticleThe Journal of biological chemistry2010
The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.
Article in The Journal of biological chemistry, 2010. 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, 39 citations in OpenAlex.
- Review
- Dual function of Zika virus NS2B-NS3 protease.PLoS pathogens · 2023Article
- Measurement of ATP utilization in RNA unwinding and RNA chaperone activities by DEAD-box helicase proteins.Methods in enzymology · 2022Article
- 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 and function of Pif1 helicase.Biochemical Society transactions · 2017Review
- Article
- Article
- ATP dependent NS3 helicase interaction with RNA: insights from molecular simulations.Nucleic acids research · 2015Article
- The linker region of NS3 plays a critical role in the replication and infectivity of hepatitis C virus.Journal of virology · 2014Article
- UK-1 and structural analogs are potent inhibitors of hepatitis C virus replication.Bioorganic & medicinal chemistry letters · 2014Article
- Yeast Pif1 helicase exhibits a one-base-pair stepping mechanism for unwinding duplex DNA.The Journal of biological chemistry · 2013Article
- Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function.Nature chemical biology · 2012Article
- Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA.Biochemistry · 2012Article
- Structure-based simulations of the translocation mechanism of the hepatitis C virus NS3 helicase along single-stranded nucleic acid.Biophysical journal · 2012Article
- Dda helicase tightly couples translocation on single-stranded DNA to unwinding of duplex DNA: Dda is an optimally active helicase.Journal of molecular biology · 2012Article
- The T4 phage SF1B helicase Dda is structurally optimized to perform DNA strand separation.Structure (London, England : 1993) · 2012Article
- RecQ helicase translocates along single-stranded DNA with a moderate processivity and tight mechanochemical coupling.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Superfamily 2 helicases.Frontiers in bioscience (Landmark edition) · 2012Review
- Single-stranded DNA translocation of E. coli UvrD monomer is tightly coupled to ATP hydrolysis.Journal of molecular biology · 2012Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Hepatitis C virus (HCV) NS3 protein has two enzymatic activities of helicase and protease that are essential for viral replication. The helicase separates the strands of DNA and RNA duplexes using the energy from ATP hydrolysis. To understand how ATP hydrolysis is coupled to helicase movement, we measured the single turnover helicase translocation-dissociation kinetics and the pre-steady-state P(i) release kinetics on single-stranded RNA and DNA substrates of different lengths. The parameters of stepping were determined from global fitting of the two types of kinetic measurements into a computational model that describes translocation as a sequence of coupled hydrolysis-stepping reactions. Our results show that the HCV helicase moves with a faster rate on single stranded RNA than on DNA. The HCV helicase steps on the RNA or DNA one nucleotide at a time, and due to imperfect coupling, not every ATP hydrolysis event produces a successful step. Comparison of the helicase domain (NS3h) with the protease-helicase (NS3-4A) shows that the most significant contribution of the protease domain is to improve the translocation stepping efficiency of the helicase. Whereas for NS3h, only 20% of the hydrolysis events result in translocation, the coupling for NS3-4A is near-perfect 93%. The presence of the protease domain also significantly reduces the stepping rate, but it doubles the processivity. These effects of the protease domain on the helicase can be explained by an improved allosteric cross-talk between the ATP- and nucleic acid-binding sites achieved by the overall stabilization of the helicase domain structure.
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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.