Specificity of the protein kinase activity associated with the hemin-controlled repressor of rabbit reticulocyte.

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Abstract
Highly purified preparations of hemin-controlled repressor of rabbit reticulocyte contain a 3'':5''-cyclic AMP-independent protein kinase activity that phosphorylates the low-MW (about 38,000) polypeptide chain of the initiation factor that forms a ternary complex with GTP and Met-tRNAf. These preparations also phosphorylate several polypeptide components of reticulocyte 40S ribosomal subunits. No significant levels of phosphorylation are observed when casein, histones, Artemia salina 40S ribosomal subunits or other initiation factor fractions are used as substrates although high levels of phosphorylation are obtained with cruder preparations of the repressor. An antibody to these highly purified preparations of repressor was obtained from the serum of immunized goats. Preincubation with immune goat IgG [immunoglobulin G] results in the neutralization of the inhibitory activity of the repressor, while normal IgG has no effect. Preincubation with immune IgG also abolishes the protein kinase activity responsible for the phosphorylation of the initiation factor and reticulocyte 40S subunits. Histone phosphorylation by crude repressor preparations is unaffected by preincubation with immune IgG.

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