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Vol 43(2009) N 6 p. 997-1003; A.A. Malygin1, Z.V. Bochkaeva2, E.I. Bondarenko3, O.A. Kossinova1, V.B. Loktev3, I.N. Shatsky2, G.G. Karpova1 Binding of the IRES of hepatitis C virus RNA to the 40S ribosomal subunit: Role of p40 1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russia2Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992, Russia 3Vector State Research Center of Virology and Biotechnology, Koltsovo, Novosibirsk Region, 630559, Russia Received - 2009-06-11; Accepted - 2009-06-11 Ribosomal protein p40 is a structural component of the eukaryotic 40S ribosomal subunit, is partly homologous to prokaryotic ribosomal protein S2, and has a long eukaryote-specific C-terminal region. The internal ribosome entry site (IRES) of the hepatitis C virus (HCV) RNA was tested for the binding to 40S ribosomal subunits deficient in p40, saturated with recombinant p40, or pretreated with monoclonal antibody (MAB) 4F6 against p40. The apparent association constant of HCV IRES binding to 40S subunits was shown to directly depend on the p40 content in the subunits. MAB 4F6 prevented HCV IRES binding to 40S subunits and blocked translation of IRES-containing RNA in a cell-free translation system. The results implicate p40 in the binding of the HCV IRES to the ribosome and, therefore, in translation initiation on HCV RNA. ribosomal protein p40 (SA), hepatitis C virus, IRES, 40S ribosomal subunit, RNA-protein interactions |
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