Protein-protein interactions within late pre-40S ribosomes.
Protein-protein interactions within late pre-40S ribosomes.
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40S 前后期核糖体内的蛋白质-蛋白质相互作用。
DOI：
10.1371/journal.pone.0016194
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发表时间：
2011-01-20
期刊：
影响因子：
3.7
通讯作者：
Karbstein K
中科院分区：
文献类型：
--
作者：
Campbell MG;Karbstein K
真核生物中的核糖体组装需要超过200个组装因子来促进和协调rRNA的转录、加工和折叠与核糖体蛋白的结合。这些组装因子中的许多在确定的时间结合和解离，产生离散的组装中间体，其中一些已经部分表征了它们的蛋白质和RNA组成。在这里，我们已经分析了蛋白质之间的相互作用的7个组装因子绑定到晚期细胞质前40 S核糖体使用重组蛋白结合试验。我们的数据表明，这些因素形成两个模块：一个包括Enp 1和出口适配器Ltv 1附近的喙结构，第二个包括激酶Rio 2，核酸酶Nob 1，和调节RNA结合蛋白Dim 2/Pno 1的头部前面。GTPase-like Tsr 1和普遍保守的甲基化酶Dim 1也与第二个模块外围相连。此外，为了进一步确定这些必需蛋白的位置，我们分析了这些组装因子与六种核糖体蛋白Rps 0，Rps 3，Rps 5，Rps 14，Rps 15和Rps 29之间的相互作用。总之，这些结果和以前的RNA-蛋白质交联数据使我们能够提出这七个组装因子结合位点的模型。此外，我们的数据表明，必需激酶Rio 2位于前核糖体颗粒的中心，并直接或间接地与其他组装因子以及细胞质40 S成熟所需的三种核糖体蛋白相互作用。这些数据表明，R102可以在调节细胞质成熟步骤中发挥核心作用。
Ribosome assembly in eukaryotic organisms requires more than 200 assembly factors to facilitate and coordinate rRNA transcription, processing, and folding with the binding of the ribosomal proteins. Many of these assembly factors bind and dissociate at defined times giving rise to discrete assembly intermediates, some of which have been partially characterized with regards to their protein and RNA composition. Here, we have analyzed the protein-protein interactions between the seven assembly factors bound to late cytoplasmic pre-40S ribosomes using recombinant proteins in binding assays. Our data show that these factors form two modules: one comprising Enp1 and the export adaptor Ltv1 near the beak structure, and the second comprising the kinase Rio2, the nuclease Nob1, and a regulatory RNA binding protein Dim2/Pno1 on the front of the head. The GTPase-like Tsr1 and the universally conserved methylase Dim1 are also peripherally connected to this second module. Additionally, in an effort to further define the locations for these essential proteins, we have analyzed the interactions between these assembly factors and six ribosomal proteins: Rps0, Rps3, Rps5, Rps14, Rps15 and Rps29. Together, these results and previous RNA-protein crosslinking data allow us to propose a model for the binding sites of these seven assembly factors. Furthermore, our data show that the essential kinase Rio2 is located at the center of the pre-ribosomal particle and interacts, directly or indirectly, with every other assembly factor, as well as three ribosomal proteins required for cytoplasmic 40S maturation. These data suggest that Rio2 could play a central role in regulating cytoplasmic maturation steps.
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