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(Received for publication, April 20, 1995) Cap-dependent binding of mRNA to the 40 S ribosomal subunit
during translational initiation requires the association of eukaryotic
initiation factor 4G (eIF4G; formerly eIF-4
Volume 270,
Number 37,
Issue of September 15, pp. 21975-21983, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
IMPLICATIONS FOR CAP-DEPENDENT AND CAP-INDEPENDENT TRANSLATIONAL
INITIATION
and p220) with other
initiation factors, notably eIF4E, eIF4A, and eIF3. Infection of cells
by picornaviruses results in proteolytic cleavage of eIF4G and
generation of a cap-independent translational state. Rhinovirus 2A
protease and foot-and-mouth-disease virus L protease were used to
analyze the association of eIF4G with eIF4A, eIF4E, and eIF3. Both
proteases bisect eIF4G into N- and C-terminal fragments termed cp
and cp
. cp was shown to contain the
eIF4E-binding site, as judged by retention on
m
GTP-Sepharose, whereas cp was bound to eIF3
and eIF4A, based on ultracentrifugal co-sedimentation. Further
proteolysis of cp by L protease produced an 18-kDa
polypeptide termed cp which retained eIF4E binding
activity and corresponded to amino acid residues 319-479 of
rabbit eIF4G. Further proteolysis of cp
yielded several
smaller fragments. cp (
887-1402) contained the
eIF4A binding site, whereas cp
(
480-886)
contained the eIF3 binding site. These results suggest that cleavage by
picornaviral proteases at residues 479-486 separates eIF4G into
two domains, one required for recruiting capped mRNAs and one for
attaching mRNA to the ribosome and directing helicase activity. Only
the latter would appear to be necessary for internal initiation of
picornaviral RNAs.
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