Assembly of the 5′ and 3′ minor domains of 16S ribosomal RNA as monitored by tethered probing from ribosomal protein S20
Assembly of the 5′ and 3′ minor domains of 16S ribosomal RNA as monitored by tethered probing from ribosomal protein S20
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DOI：
10.1016/j.jmb.2007.10.083
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发表时间：
2008-02-08
影响因子：
5.6
通讯作者：
Culver, Gloria M.
中科院分区：
文献类型：
--
作者：
Dutca, Laura M.;Culver, Gloria M.
核糖体蛋白（r-protein）S20是一种主要的结合蛋白。因此，它直接和独立地与最小颗粒中的16 S核糖体RNA（rRNA）的5'结构域以及3'次要结构域和完全组装的30 S亚基相互作用。在r-蛋白S20和16 S rRNA的5'结构域之间观察到的相互作用是相当广泛的，而在r-蛋白S20和3'次要结构域之间观察到的相互作用明显更有限。在这项研究中，直接羟基自由基探测介导的Fe（II）衍生的S20蛋白质被用来监测折叠的16 S rRNA在r-蛋白质协会和30 S亚基组装。在最小的复合物[16 S rRNA和Fe（II）-S20]和完全组装的30 S亚基含有相同的Fe（II）衍生蛋白质的裂解模式的分析显示有趣的相似性和差异。这些结果表明，这两个结构域，5'和3'次要的，是组织相对于S20在不同阶段的组装。5'结构域在比3'次要结构域更不复杂的核糖核蛋白颗粒中获得与在成熟亚基中观察到的相同的结构。这些结果类似于通过5 '至3'方向组装模型预测的亚基组装。(C)2007爱思唯尔有限公司版权所有。
The ribosomal protein (r-protein) S20 is a primary binding protein. As such, it interacts directly and independently with the 5' domain as well as the 3' minor domain of 16S ribosomal RNA (rRNA) in minimal particles and the fully assembled 30S subunit. The interactions observed between r-protein S20 and the 5' domain of 16S rRNA are quite extensive, while those between r-protein S20 and the 3' minor domain are significantly more limited. In this study, directed hydroxyl radical probing mediated by Fe(II)-derivatized S20 proteins was used to monitor the folding of 16S rRNA during r-protein association and 30S subunit assembly. An analysis of the cleavage patterns in the minimal complexes [16S rRNA and Fe(II)-S20] and the fully assembled 30S subunit containing the same Fe(II)-derivatized proteins shows intriguing similarities and differences. These results suggest that the two domains, 5' and 3' minor, are organized relative to S20 at different stages of assembly. The 5' domain acquires, in a less complex ribonucleoprotein particle than the 3' minor domain, the same architecture as observed in mature subunits. These results are similar to what would be predicted of subunit assembly by the 5'-to-3' direction assembly model. (C) 2007 Elsevier Ltd. All rights reserved.