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(Received for publication, September 16, 1996)
,
,
and
From the Eukaryotic initiation factor 3 (eIF3) is a large
multisubunit complex that stabilizes the ternary complex,
eIF2·GTP·tRNAiMet, and promotes
mRNA binding to the 40 S ribosomal subunit. eIF3 also functions as
a ribosome subunit anti-association factor. The molecular mechanisms by
which eIF3 exerts these functions are poorly understood. We describe
here the cloning of the cDNA encoding the human homologue of the
yeast eIF3 subunit Prt1. The human PRT1 cDNA encodes a protein of
predicted molecular mass of 98.9 kDa that migrates at 116 kDa on
SDS-polyacrylamide gels. Human and yeast Prt1 share 31% identity and
50% similarity at the amino acid level. The homology is distributed
throughout the entire protein, except for the amino terminus, and is
particularly high in the central portion of the protein, which contains
a putative RNA recognition motif. hPrt1 is recognized by an antibody
raised against eIF3, and an affinity-purified antibody to recombinant hPrt1 recognizes a protein migrating at 116 kDa in a purified eIF3
preparation. Far Western analysis shows that hPrt1 interacts directly
with the p170 subunit of eIF3. Mapping studies identify the RNA
recognition motif as the region required for association with p170.
Taken together, these experiments demonstrate that hPrt1 is a component
of eIF3. Our data, combined with those of Hershey and co-workers,
suggest that mammalian eIF3 is composed of at least 10 subunits: p170,
p116 (hPrt1), p110, p66, p48, p47, p44, p40, p36, and p35.
Department of Biochemistry and McGill Cancer
Centre, McGill University, Montréal, Québec, Canada H3G 1Y6
and 
Human Genome Science Inc., Rockville, Maryland 20850
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