| Literature DB >> 18155046 |
Vaishnavi Rajagopal1, Smita S Patel.
Abstract
The nonstructural NS3 protein of the hepatitis C virus is a multifunctional enzyme with an N-terminal serine protease activity and a C-terminal helicase activity. The helicase is capable of unwinding both DNA and RNA duplexes; however, the overall processivity of the helicase is fairly low. We show here that single-strand binding (SSB) proteins enhance the unwinding processivity of both the NS3 helicase domain (NS3h) and the full-length protease-helicase NS3-4A. The detailed study of the effect of SSB on the DNA unwinding activity of NS3h indicates that the SSB stabilizes the helicase at the unwinding junction and prevents its dissociation. These results suggest a potential role for either cellular or virus-encoded SSB protein in improving the processivity of the NS3 in vivo.Entities:
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Year: 2007 PMID： 18155046 PMCID： PMC2249756 DOI： 10.1016/j.jmb.2007.10.070
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469