Kl. Block et al., CHARACTERIZATION OF CDNAS ENCODING THE P44 AND P35 SUBUNITS OF HUMAN TRANSLATION INITIATION-FACTOR EIF3, The Journal of biological chemistry, 273(48), 1998, pp. 31901-31908
Eukaryotic translation initiation factor 3 (eIF3) is a large multisubu
nit complex that plays a central role in the initiation of translation
. It binds to 40 S ribosomal subunits resulting in dissociation of 80
S ribosomes, stabilizes initiator methionyl-tRNA binding to 40 S subun
its, and is required for mRNA binding. eIF3 has an aggregate molecular
mass of similar to 600 kDa and comprises at least 10 subunits, The cD
NAs encoding eight of the subunits have been cloned previously (p170,
pile, p110, p66, p48, p47, p40, and p36), Here we report the cloning a
nd characterization of human cDNAs encoding two more subunits of human
eIF3, namely eIF3-p44 and eIF3-p35. These proteins are immunoprecipit
ated by affinity-purified anti-eIF3-p170 antibodies, indicating they a
re components of the eIF3 complex. Far Western analysis shows that eIF
3-p44 interacts strongly and specifically with the eIF3-p170 subunit,
and weakly with p116/p110, p66, p40, and itself. eIF3-p44 contains an
RNA recognition motif near its C terminus. Northwestern blotting shows
that eIF3-p44 binds 18 S rRNA and beta-globin mRNA. Possession of clo
ned cDNAs encoding all 10 subunits of eIF3 provides the tools necessar
y to elucidate the functions of the individual subunits and the struct
ure of the eIF3 complex.