The primary structure of the human ribosomal protein S6 derived from a cloned cDNA

Polyclonal antibodies directed against a synthetic octapeptide of the cAMP-dependent phosphorylation site of the ribosomal protein S6 of rat liver were used to screen a lambda gt11 cDNA expression library of human lymphoblasts. An S6 specific clone was isolated. It consists of the complete coding sequence of 747 base pairs and the 3'noncoding region of 40 base pairs. The sequence of 249 amino acids was deduced from the nucleotide sequence. The amino- and carboxyl-terminal regions are almost identical to the reported partial peptide sequences of rat liver S6. The yeast protein S10 is homologous to the human S6 with the exception of 3 amino acid insertions an a carboxyl-terminal extension of 10 amino acids within the human S6. The only two phosphorylation sites at the carboxyl terminus of yeast S10 are homologous to the two cAMP-dependent site in human S6. Since there are additional phosphorylation sites in mammalian S6, one can assume that they are located in the cluster of 5 serines wi thin the carboxyl-terminal extension. The sequence comparison of these two ribosomal proteins from evolutionarily distant eucaryotes, such as man and yeast, indicates that the structure and probably the function of the phosphoprotein S6 of the small ribosomal subunit has been highly conserved. The expression of the S6 gene has been investigated in proliferating lymphocytes stimulated by concanavalin A. During all stages of lymphoblast development the level of S6 mRNA appeared to be similar