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J Biol Chem, Vol. 273, Issue 13, 7579-7587, March 27, 1998
From the Departments of Biochemistry and § Veteran's
Affairs Medical Center and of Medicine, Case Western Reserve
University, Cleveland, Ohio 44106-4935
A new protein with translational activity has
been identified on the basis of its ability to stimulate translation in
an in vitro globin synthesis assay deficient in eukaryotic
initiation factor (eIF) 4B and eIF4F. This protein has been purified to
greater than 80% homogeneity from rabbit reticulocyte lysate and has
been given the name eIF4H. eIF4H was shown to stimulate the in
vitro activities of eIF4B and eIF4F in globin synthesis, as well
as the in vitro RNA-dependent ATPase activities
of eIF4A, eIF4B, and eIF4F. Three tryptic fragments of eIF4H yielded
amino acid sequences that were 100% identical to a human sequence
found in the GeneBankTM that codes for a previously
uncharacterized protein (HUMORFU_1). The calculated molecular weight of
the protein encoded by this sequence, its predicted cyanogen bromide
fragmentation, and calculated isoelectric point are all consistent with
those determined experimentally for eIF4H. Also, the presence of an RNA
recognition motif within HUMORFU_1 suggests that eIF4H may interact
with mRNA. We conclude that this newly characterized protein,
eIF4H, functions to stimulate the initiation of protein synthesis at
the level of mRNA utilization, and is encoded by the gene for
HUMORFU_1.
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