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The role of the basic N-terminal region of protein L18 in 5S RNA–23S RNA complex formation

机译:蛋白质L18基本N-末端区域在5S RNA-23S RNA复合物中的作用

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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 Ll8 fragment. Two possible models for the mechanism of RNA-RNA assembly are proposed.
机译:在结合5S RNA的三种蛋白质,L5,L18和L25中,前两者效果5S RNA与23S RNA的相互作用。我们使用胰蛋白酶作为探针,以研究该RNA-RNA组件中蛋白质的作用,其中:(1)在具有5S RNA的络合物中,胰蛋白酶可以获得L18的高碱性N-末端区域。此可访问性不受L25的影响。然而,其存在对于刺激L5结合至关重要。 (2)在5S中,RNA-蛋白-23S RNA络合物蛋白质L5和L18均耐受蛋白水解。 (3)在L5和C末端LL8片段存在下,没有5S RNA-23S RNA复合物形成。提出了用于RNA-RNA组件的两个可能模型。

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