Phosphorylation in vivo of non-ribosomal proteins from native 40 S ribosomal particles of Krebs II mouse ascites-tumour cells.
Four non-ribosomal proteins from native 40 S ribosomal subunits with mol.wts. of 110 000, 84 000, 68 000 and 26 000 were phosphorylated in vivo when ascites cells were incubated in the presence of [32P]Pi. The 110 000-, 84 000- and 26 000-dalton proteins are identical with phosphorylated products from native 40 S subunits after phosphorylation in vitro by a cyclic nucleotide-independent protein kinase. Phosphoserine was the major phosphorylated amino acid of the proteins phosphorylated in vivo and in vitro.
D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D002287:Carcinoma, Krebs 2 / Q000378:metabolism*; D002460:Cell Line; D051379:Mice; D008970:Molecular Weight; D010448:Peptide Initiation Factors / Q000378:metabolism*; D010766:Phosphorylation; D012269:Ribosomal Proteins / Q000378:metabolism*
D000596:Amino Acids; D010448:Peptide Initiation Factors; D012269:Ribosomal Proteins