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1 Department of Microbiology and Immunology, Morse
Institute for Molecular Genetics, State University of New York Health
Science Center at Brooklyn, Brooklyn, New York 11203;
2 A.N.
Belozersky Institute of Physico-Chemical Biology, Moscow State
University, 119899 Moscow, Russia;
3 Department of
Biochemistry, University of Cambridge, Cambridge, CB2 1QW, UK
Initiation of translation of hepatitis C virus and classical swine
fever virus mRNAs results from internal ribosomal entry. We
reconstituted internal ribosomal entry in vitro from purified translation components and monitored assembly of 48S ribosomal preinitiation complexes by toe-printing. Ribosomal subunits (40S) formed stable binary complexes on both mRNAs. The complex structure of
these RNAs determined the correct positioning of the initiation codon
in the ribosomal "P" site in binary complexes. Ribosomal binding
and positioning on these mRNAs did not require the initiation factors
eIF3, eIF4A, eIF4B, and eIF4F and translation of these mRNAs was not
inhibited by a trans-dominant eIF4A mutant. Addition of
Met-tRNAiMet, eIF2, and GTP to
these binary ribosomal complexes resulted in formation of 48S
preinitiation complexes. The striking similarities between this
eukaryotic initiation mechanism and the mechanism of translation
initiation in prokaryotes are discussed.
[Key Words: Hepatitis C virus; mRNA; translation initiation; protein synthesis; ribosome]
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