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J Biol Chem, Vol. 273, Issue 29, 18599-18604, July 17, 1998
From the A complex of eukaryotic initiation factors (eIFs)
4A, 4E, and 4G (collectively termed eIF4F) plays a key role in
recruiting mRNAs to ribosomes during translation initiation. The
site of ribosomal entry onto most mRNAs is determined by
interaction of the 5'-terminal cap with eIF4E; eIFs 4A and 4G may
facilitate ribosomal entry by modifying mRNA structure near the cap
and by interacting with ribosome-associated factors. eIF4G recruits
uncapped encephalomyocarditis virus (EMCV) mRNA to ribosomes
without the involvement of eIF4E by binding directly to the
~450-nucleotide long EMCV internal ribosome entry site (IRES). We
have used chemical and enzymatic probing to map the eIF4G binding site
to a structural element within the J-K domain of the EMCV IRES that
consists of an oligo(A) loop at the junction of three helices. The
oligo(A) loop itself is not sufficient to form stable complexes with
eIF4G since alteration of its structural context abolished its
interaction with eIF4G. Addition of wild type or
trans-dominant mutant forms of eIF4A to binary IRES·eIF4G
complexes did not further alter the pattern of chemical/enzymatic
modification of the IRES.
Translation Eukaryotic Initiation Factor 4G Recognizes a Specific
Structural Element within the Internal Ribosome Entry Site of
Encephalomyocarditis Virus RNA
§,§,
A. N. Belozersky Institute of
Physico-Chemical Biology, Moscow State University, 119899 Moscow,
Russia and § Department of Microbiology and Immunology,
Morse Institute for Molecular Genetics, State University of New York
Health Science Center at Brooklyn, Brooklyn, New York 11203-2098
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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