Phosphorylation of acidic ribosomal proteins from rabbit reticulocytes by a ribosome-associated casein kinase.
Two acidic proteins from 80-S ribosomes were isolated and purified to homogeneity. The purified acidic proteins could be phosphorylated by casein kinase using [gamma-32P]ATP and [gamma-32P]GTP as a phosphoryl donor. The proteins became phosphorylated in situ, too. Sodium dodecyl sulfate polyacrylamide gel analysis of the purified acidic proteins and 80-S particles showed identical phosphoproteins in the 16 000 dalton region.
D000255:Adenosine Triphosphate; D000818:Animals; D002364:Caseins; D006160:Guanosine Triphosphate; D008970:Molecular Weight; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism
D002364:Caseins; D012269:Ribosomal Proteins; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D011494:Protein Kinases