Newberry V, Garrett R A
Nucleic Acids Res. 1980 Sep 25;8(18):4131-42. doi: 10.1093/nar/8.18.4131.
Of the three proteins, L5, L18 and L25, which bind to 5S RNA, the former two effect the interaction of 5S RNA with 23S RNA. We have used trypsin as a probe to investigate the roles of the proteins in this RNA-RNA assembly, with the following results: (1) In complexes with 5S RNA, the highly basic N-terminal region of L18 is accessible to trypsin. This accessibility is unaffected by L25. However, its presence is essential for stimulating L5 binding. (2) In 5S RNA-protein-23S RNA complexes proteins L5 and L18 are both strongly resistant to proteolysis. (3) No 5S RNA-23S RNA complex formation occurs in the presence of L5 and the C-terminal L18 fragment. Two possible models for the mechanism of RNA-RNA assembly are proposed.
在与5S RNA结合的三种蛋白质L5、L18和L25中，前两种蛋白质影响5S RNA与23S RNA的相互作用。我们使用胰蛋白酶作为探针来研究这些蛋白质在这种RNA-RNA组装中的作用，结果如下：（1）在与5S RNA形成的复合物中，L18高度碱性的N端区域可被胰蛋白酶作用。这种可及性不受L25的影响。然而，L25的存在对于刺激L5的结合至关重要。（2）在5S RNA-蛋白质-23S RNA复合物中，蛋白质L5和L18都对蛋白水解具有很强的抗性。（3）在L5和L18 C端片段存在的情况下，不会形成5S RNA-23S RNA复合物。提出了两种关于RNA-RNA组装机制的可能模型。
