In vivo isotope incorporation patterns into HeLa ribosomal proteins

When cells were incubated with L-[35S] methionine plus L-[Me-3H] methionine, it was found that at least four ribosomal proteins had 3H/35S ratios higher than the rest of the ribosomal proteins, suggesting that they were methylated. The rate of apparent methylation paralleled the rate of amino acid incorporation. Amino acid incorporation into ribosomal proteins revealed several rapidly labeled components. When 3H-labeled amino acid incorporation was chased for 10 min with an excess of non-radioactive amino acids, several proteins reached at least 60% of the specific activity they showed after 150 min of chase. The time lapse between the onset of 3H-labeled amino acid incorporation and arrival at its plateau appeared to differ among various ribosomal proteins of a subunit, suggesting a heterogeneity in the pools of ribosomal proteins.