期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 376, 期 1, 页码 69-79出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.10.070
关键词
HCV; unwinding; NS3; SSB; processivity
资金
- NIGMS NIH HHS [R01 GM055310-12, GM55310, R01 GM055310] Funding Source: Medline
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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