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(Received for publication, November 2, 1995; and in revised form, January 23, 1996)
The cap-binding eukaryotic initiation factor, eIF4E, is a key
target for the regulation of translation in mammalian cells and is
widely thought to be present at very low molar concentrations. Here we
present observations with the reticulocyte lysate that challenge this
view. When reticulocyte ribosomes are harvested by centrifugation, most
(
75%) of the eIF4E remains in the postribosomal supernatant (PRS).
In a reconstituted translation system we find that the
ribosome-associated eIF4E alone can sustain much of the overall
activity, suggesting that much of the factor in the PRS is functionally
redundant. Consistent with this, our estimates of eIF4E in the
reticulocyte lysate reveal much higher concentrations than previously
reported. The association of a small proportion of eIF4E with the
ribosome fraction appears to be functional and dependent on interaction
with the factor eIF4G. This fraction of eIF4E is, as expected, more
highly phosphorylated than that in the PRS; however, at least half the
total phosphorylated eIF4E in reticulocyte lysate translation systems
resides in the PRS fraction, suggesting that, while phosphorylation may
enhance activity, it is not in itself sufficient to promote utilization
of the factor. We also show that the eIF4E-binding factor, eIF4E-BP1 or
PHAS-I, which regulates eIF4E activity in insulin-responsive cells, is
present in the reticulocyte PRS at an approximately 1:1 molar ratio
relative to eIF4E and demonstrate by co-immunoprecipitation studies
that the binding of PHAS-I and eIF4G to eIF4E is mutually exclusive.
These data are consistent with a potential regulatory role for PHAS-I
in the reticulocyte lysate.
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