ribosomal subunits. sharp reduction of decency in the treatment of postdoctoral fellows. We the cellular content of 43S pre initiation complex. and have subsequently aspired, within the constraints of our the phosphorylation of elF-2ex and inhibition of eIF-2B ability, to pattern our behavior in accord with this expe­ [15-17]. Neither translational elongation nor peptide rience. Our current research involving the control of chain termination appeared to be affected in these ex­ protein synthesis at mRNA translation embodies much periments, since average ribosomal transit times and the methionylation of tRNA;met were not altered. Amino of the familiar in protein phosphorylation with some new twists that we shall highlight in this article with our acid incorporation was unaffected during the period of 2 associate. Dr. Prostko. Ca+ release prior to suppression of initiation.