The acidic sequence of the NS4A cofactor regulates ATP hydrolysis by the HCV NS3 helicase |
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Authors: | Sergey A. Shiryaev Andrei V. Chernov Tatiana N. Shiryaeva Alexander E. Aleshin Alex Y. Strongin |
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Affiliation: | Inflammatory and Infectious Disease Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. |
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Abstract: | In flaviviruses and hepatitis C virus (HCV), the NS3 gene encodes the N-terminal protease (NS3pro) and the C-terminal helicase (NS3hel). In HCV, the downstream NS4A is required for the NS3pro activity and exhibits a conserved EFDEMEE motif. To identify the role of this motif, we compared the ATPase and helicase activities of NS3 alone with those of the NS3-NS4A constructs. Our results suggest that the EFDEMEE motif is essential for regulating the ATPase activity of NS3hel. It is likely that this motif interferes with the ATP-binding site of NS3hel. It is becoming clear that NS4A functions as a cofactor of both proteinase and helicase in HCV. |
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