Bommer U A, Bielka H, Henske A, Kärgel H J
Acta Biol Med Ger. 1981;40(9):1105-10.
The evidence that protein S6 of rat liver ribosomes is involved in P-site functions and that this protein is the main target of the small subunit for in vivo phosphorylation suggests that S6 phosphorylation may contribute to the regulation of protein synthesis. Therefore, we have studied the activity of small ribosomal subunits with unphosphorylated and phosphorylated protein S6 in Met-tRNAf binding. The results described in this paper show that at least under in vitro conditions S6 phosphorylation does obviously not influence the activity of small ribosomal subunits for eIF-2 dependent binding of initiator-tRNA.
大鼠肝脏核糖体的蛋白质S6参与P位点功能，且该蛋白质是体内磷酸化时小亚基的主要作用靶点，这一证据表明S6磷酸化可能有助于蛋白质合成的调控。因此，我们研究了未磷酸化和磷酸化的蛋白质S6的小核糖体亚基在甲硫氨酸-tRNAf结合中的活性。本文所述结果表明，至少在体外条件下，S6磷酸化显然不会影响小核糖体亚基对eIF-2依赖的起始tRNA结合的活性。
