Molecular Dissection of the Ribosomal Protein Complex that Plays a as Drive Part of Translation apparatus

所有生物体内的核糖体都有一个独特的由核糖体蛋白复合物组成的柔性结构，称为柄，它在核糖体的功能中起着至关重要的作用。在本研究课题中，我们通过生化和晶体学分析研究了超嗜热古菌核糖体柄的结构和功能。结果表明，该古菌的茎部由aP0和aP1组成，形成七聚体复合物aP0(aP1)_2(aP1)_2(aP1)_2 (aP1)_2(aP1)_2，其c端序列由aP1和aP0共享，直接与翻译因子结合。我们得出结论，复合物中aP1/aP0的7个c端尾拷贝参与了翻译因子在核糖体上的有效募集。

Ribosomes in all organisms have a unique flexible structure composed of ribosomal protein complex, termed the stalk, which plays a crucial role in ribosome function. In this research subject, we have investigated the structure and function of the ribosomal stalk in a hyperthermophilic archaeon by biochemical and crystallographic analyses. The results showed that the archaeal stalk is composed of aP0 and aP1, which form the heptameric complex aP0(aP1)_2(aP1)_2(aP1)_2, and that the C-terminal sequence, which is shared by aP1 and aP0, directly binds to translation factors. We concluded that the 7 copies of C-terminal tails of aP1/aP0 in the complex participate in efficient recruitment of translation factors onto the ribosome.