title: Distinct modes of poliovirus polyprotein initiation in vitro.
abstract: 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.
authors.affiliation: A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, U.S.S.R.
authors.forename: T V
authors.initials: TV
authors.lastname: Pestova
authors.forename: S V
authors.initials: SV
authors.lastname: Maslova
authors.forename: V K
authors.initials: VK
authors.lastname: Potapov
authors.forename: V I
authors.initials: VI
authors.lastname: Agol
mesh_terms: 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
chemical_list: D012367:RNA, Viral; D014764:Viral Proteins; D004722:Endoribonucleases; D016914:Ribonuclease H