Interaction of synthetic polynucleotides with small rat liver ribosomal subunits possessing low and highly phosphorylated protein S6.

The interaction of some synthetic mRNAs (polyuridylate, polyadenylate, polycytidylate) with small rat liver ribosomal subunits which have protein S6 in different states of phosphorylation was studied by BioGel column chromatography, affinity chromatography on poly(U)-Sepharose 4B, and continuous diafiltration at 4 degrees C. 40-S subunits with low phosphorylated protein S6 (isolated from normal liver) and small subunits with highly phosphorylated protein S6 (from galactosamine-, thioacetamide-, dimethylnitrosamine-, puromycin-, and cycloheximide-treated livers) bind initially equal amounts of poly(U) but the dissociation of the radioactive polyuridylate occurs much more rapidly and to a greater extent from the low than from the highly phosphorylated type of subunits. From control- and galactosamine-4-S subunits 62% and 22%, respectively, of originally bound [3H]poly(U) was removed. The release of initially bound poly(A) from 40-S subunits of galactosamine-treated liver ws retarded but reached finally the same level as with control liver ribosomal subunits (removal of 40% of bound [3H]poly(A)). No differences between low and highly phosphorylated subunits were observed with poly(C). If the dissociation reaction was performed at 22 degrees C instead of 4 degrees C the differences in the release of poly(U) described above disappeared.