Distinct modes of poliovirus polyprotein initiation in vitro.
RNAs of poliovirus type 1 and type 3 were translated in extracts from Krebs-2 cells after annealing with oligodeoxyribonucleotides complementary to different sites in the 5'-untranslated region (5'-UTR). Due to a high level of endogenous RNase H activity in the extracts, such RNAs appeared to be efficiently 5'-truncated prior to translation. The observed levels of initiation on differently truncated templates suggested that a region in the middle of the poliovirus 5'-UTR is essential for the cap-independent initiation of viral polyprotein synthesis. The data reported here, in conjunction with the results from other laboratories, permitted to relate the essential cis-acting control elements to the 5'-UTR secondary structure domains defined previously (E.V. Pilipenko et al., Virology 168, 201-209). However, the removal of these domains activated another mode of polyprotein initiation, which appeared to require another set of translation initiation factors.
Pestova
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A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, U.S.S.R.
Maslova
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Potapov
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VK
Agol
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D001483:Base Sequence; D004722:Endoribonucleases / Q000378:metabolism; D015151:Immunoblotting; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D017955:Poliovirus / Q000235:genetics* / Q000472:pathogenicity; D014176:Protein Biosynthesis; D012367:RNA, Viral / Q000235:genetics*; D016914:Ribonuclease H; D014764:Viral Proteins / Q000235:genetics*; D014774:Virulence
D012367:RNA, Viral; D014764:Viral Proteins; D004722:Endoribonucleases; D016914:Ribonuclease H