Abstract
MODIFICATION of ribosomal proteins has been suggested as a mechanism controlling protein biosynthesis1. In vivo and in vitro phosphorylation of eukaryotic ribosomal proteins has been described and its possible functional relevance discussed2–5. Two-dimensional polyacrylamide gel electrophoresis has shown that only one, small ribosomal subunit protein, S6, is phosphorylated in rat liver6. The number of phosphoserine residues in this protein increases by an order of magnitude during liver regeneration6 and also after administration of inhibitors of protein synthesis7. In addition, when Escherichia coli is infected with bacteriophage T7, various host cell proteins, including some ribosomal proteins, are phosphorylated8. In our search for possible regulatory changes in the protein synthesising apparatus of virus-infected cells, we have now examined the phosphorylation of ribosomal proteins in HeLa cells infected with vaccinia virus.
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