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  • Title: Specificity and mechanism analysis of hepatitis C virus RNA-dependent RNA polymerase.
    Author: Johnson RB, Sun XL, Hockman MA, Villarreal EC, Wakulchik M, Wang QM.
    Journal: Arch Biochem Biophys; 2000 May 01; 377(1):129-34. PubMed ID: 10775451.
    Abstract:
    The RNA-dependent RNA polymerase encoded by the hepatitis C virus (HCV) NS5B gene has been expressed as a nonfusion protein in bacterial cells and purified to homogeneity using sequential chromatographic columns. The purified NS5B protein exhibited RNA-dependent RNA polymerase activity using poly(A) template and the K(m) and V(max) were determined as 8.4 microM and 1976 pmol/mg-min, respectively. This full-length NS5B protein exhibited much stronger binding affinity toward the 30-mer poly(G) than other homopolymeric RNAs of the same size. For the first time, we demonstrate that the HCV NS5B was able to bind various ribonucleotides. Using a panel of oligonucleotides varying in length, we studied the NS5B catalytic efficiency and proposed the size of the NS5B active site to be 8-10 nucleotides. The multifunctional nature of NS5B protein is also discussed and compared with other viral RNA polymerases.
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