The DExH Protein NPH-II is processive and directional motor for unwinding RNA
Article Abstract:
DExH/D proteins are required for the replication of certain viruses and are thus targets for the development of therapeutics. It is proposed that DExH/D proteins couple NTP hydrolysis to RNA conformational change in complex macromolecular assemblies. It is shown that DExH protein NPH-II unwinds RNA duplexes, and a quantitative connection between ATP utilization and helicase processivity is observed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase
Article Abstract:
A time-resolved approach is used to monitor the microscopic behavior of a NS3 helicase at each nucleotide of a duplex substrate. It demonstrates that NS3 unwinds RNA through fast rippling and local pausing that occurs with regular spacing along the duplex substrate.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP
Article Abstract:
Study is conducted to show that the cyclic movement of hepatitis C virus (NS3) is coordinated by ATP in discrete steps of 11(plusmn)3 base pairs, and that actual unwinding occurs in rapid smaller sub steps of 3.6(plusmn)1.3 base pairs, also triggered by ATP bindings, indicating that NS3 move like an inchworm. This ATP-coupling mechanism is likely to be applicable to other non-hexameric helicases involved in many essential cellular functions.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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