A low level of general ribosomal protein synthesis occurs during embryonic cleavage of Strongylocentrotus purpuratus. Wide differences in specific activities indicate that the synthesis or turnover of individual ribosomal proteins occurs at different rates and is not coordinated with respect to each other. In general, proteins with the greatest specific radioactivities are those in the higher molecular weight range. Experiments with actinomycin D indicate that the production of most of the ribosomal proteins is not coordinated with that of rRNA, and probably occurs on maternal mRNAs.
A comparison of early and late cleavage stages shows an overall similarity in labelling patterns, although some differences in specific activities are detectable.
Control experiments show that newly formed proteins cannot be removed from ribosomes by washing in 1M salt. A number of possible sources of artifacts, including the occurence of nascent peptide-associated proteins, artifactual complexes between ribosomes and soluble proteins as well as bacterial contamination, have been ruled out.
The results support a dynamic model for ribosome structure with respect to at least some of the protein constituents.
Ribosomal Protein Actinomycin Specific Radioactivity Labelling Pattern Cleavage Stage
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