An in vivo and in vitro phosphorylation of yeast ribosomal proteins.
Phosphorylation of yeast ribosomal proteins has been demonstrated in vivo and in vitro. 32-P-labelled product represents an ester-linked class of phosphoprotein. Acrylamide-gel electrophoresis has shown that in both types of experiments radioactive proteins migrate similarly; this might indicate that closely related groups of proteins become phosphorylated in vivo and in vitro. In the presence of [32-P] ATP the amount of covalently bound phosphate was 1.0 - 1.2 moles/mole of ribosome. The phosphorylation of ribosomal proteins did not appreciably affect the activity of ribosomes in a cell-free protein-synthesizing system containing poly(U) and elongation factors.
D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000378:metabolism*; D008274:Magnesium / Q000494:pharmacology; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects; D010445:Peptide Elongation Factors; D010750:Phosphoproteins / Q000096:biosynthesis*; D011092:Polyethylene Glycols; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*
D005656:Fungal Proteins; D010445:Peptide Elongation Factors; D010750:Phosphoproteins; D011092:Polyethylene Glycols; D011494:Protein Kinases; D008274:Magnesium