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J. Biol. Chem., Vol. 259, Issue 11, 6708-6711, 06, 1984
RL Matts and IM London
The capacity of whole reticulocyte lysates to catalyze the dissociation of
exogenously added eIF-2 X [3H]GDP was determined as a measure of their
reversing factor (RF) activity in the recycling of eIF-2 for the
maintenance or restoration of protein synthesis. We have examined the
relationship of RF activity to the protein synthetic activity of the lysate
under normal conditions and on inhibition of protein synthesis by heme
deficiency, double-stranded RNA, or oxidized glutathione. A direct
correlation was found between a lysate's capacity to synthesize protein and
its ability to stimulate the dissociation of eIF-2 X GDP. These findings
further support the proposed mechanism by which the phosphorylation of only
30-40% of the eIF-2(alpha) in the lysate renders the limiting amount of RF
present non-functional, impairing the recycling of eIF-2 and thereby
inhibiting the initiation of protein synthesis.
The regulation of initiation of protein synthesis by phosphorylation of eIF-2(alpha) and the role of reversing factor in the recycling of eIF-2
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