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首页> 外文期刊>Journal of Molecular Biology >Ribosomal Protein L11 Selectively Stabilizes a Tertiary Structure of the GTPase Center rRNA Domain
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Ribosomal Protein L11 Selectively Stabilizes a Tertiary Structure of the GTPase Center rRNA Domain

机译：核糖体蛋白L11选择性地稳定GTPase中心RRNA结构域的三级结构

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摘要

The GTPase Center (GAC) RNA domain in bacterial 23S rRNA is directly bound by ribosomal protein L11, and this complex is essential to ribosome function. Previous cocrystal structures of the 58-nucleotide GAC RNA bound to L11 revealed the intricate tertiary fold of the RNA domain, with one monovalent and several divalent ions located in specific sites within the structure. Here, we report a new crystal structure of the free GAC that is essentially identical to the L11-bound structure, which retains many common sites of divalent ion occupation. This new structure demonstrates that RNA alone folds into its tertiary structure with bound divalent ions. In solution, we find that this tertiary structure is not static, but rather is best described as an ensemble of states. While L11 protein cannot bind to the GAC until the RNA has adopted its tertiary structure, new experimental data show that L11 binds to Mg2+-dependent folded states, which we suggest lie along the folding pathway of the RNA. We propose that L11 stabilizes a specific GAC RNA tertiary state, corresponding to the crystal structure, and that this structure reflects the functionally critical conformation of the rRNA domain in the fully assembled ribosome. (C) 2019 Elsevier Ltd. All rights reserved.
机译：细菌23s rRNA中的GTPase中心（GAC）RNA结构域通过核糖体蛋白L11直接结合，并且该复合物对核糖体功能至必要。与L11结合的58核苷酸GAC RNA的先前共聚结构揭示了RNA结构域的复杂的叔折叠，其中一种单价和位于结构内的特异性位点的几种二价管。这里，我们报告了一种新的GAC的新晶体结构，其基本上与L11边界结构相同，其保留了许多常见的离子占用位点。这种新结构表明，用结合的二价离子单独折叠成其三级结构。在解决方案中，我们发现这个三级结构不是静态的，而是最好被描述为各国的集合。虽然L11蛋白不能与GAC结合直到RNA采用其三级结构，但新的实验数据表明L11与Mg2 +依赖性折叠状态结合，我们建议沿RNA的折叠途径呈现。我们提出L11稳定对应于晶体结构的特异性GAC RNA三级状态，并且该结构反映了完全组装的核糖体中RRNA结构域的功能临界构象。 （c）2019 Elsevier Ltd.保留所有权利。

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