Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 376, Issue 1, Pages 69-79Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.10.070
Keywords
HCV; unwinding; NS3; SSB; processivity
Categories
Funding
- NIGMS NIH HHS [R01 GM055310-12, GM55310, R01 GM055310] Funding Source: Medline
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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. (C) 2007 Elsevier Ltd. All rights reserved.
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