| Autor: |
Malygin AA, Bochkaeva ZV, Bondarenko EI, Kosinova OA, Loktev VB, Shatskiĭ IN, Karpova GG |
| Jazyk: |
ruština |
| Zdroj: |
Molekuliarnaia biologiia [Mol Biol (Mosk)] 2009 Nov-Dec; Vol. 43 (6), pp. 1070-6. |
| Abstrakt: |
Ribosomal protein p40 is a structural component of the 40S ribosomal subunit, which is partially homologuos to prokaryotic ribosomal protein S2 and has a long eukaryote-specific C-terminal region. In the present work, we have studied the binding of the Internal Ribosome Entry Site (IRES) of the hepatitis C virus (HCV) RNA to the 40S ribosomal subunit either deficient on protein p40, or saturated with the recombinant p40, or pre-bound to monoclonal antibodies (MAB) 4F6 against p40. It was shown that the apparent association constant of HCV IRES binding to 40S subunits directly depends on p40 content in the subunits. Binding of MAB 4F6 against p40 to 40S subunits prevented the HCV IRES binding by the subunits and blocked translation of the IRES-containing RNA in cell-free translation system. The data obtained point to the involvement of the ribosomal protein p40 in the binding of the HCV IRES by ribosomes and therefore in initiation of translation of RNA of this virus. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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