RNA tertiary structure and cooperative assembly of a large ribonucleoprotein complex
RNA tertiary structure and cooperative assembly of a large ribonucleoprotein complex
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DOI：
10.1016/j.jmb.2004.09.009
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发表时间：
2004-11-19
影响因子：
5.6
通讯作者：
Williamson, JR
中科院分区：
文献类型：
--
作者：
Recht, MI;Williamson, JR
控制多蛋白核糖核蛋白复合物有序组装的机制尚不清楚。细菌核糖体小亚基的体外重建为有序组装的详细研究提供了一个易于处理的系统。我们对 30S 核糖体亚基平台组装过程中核糖体蛋白与 16S rRNA 的分级结合进行了定量热力学描述。 S8、S11、S15 和 S6:S18 异二聚体与 16 S rRNA 中心结构域的结合已使用等温滴定量热法和凝胶迁移率位移测定法单独或组合测量。焓和自由能测量均证明了 S15 和 S6:S18 异二聚体的协同结合，但没有观察到 S8 或 S11 的协同结合。结果定义了描述协作平台组装的热力学框架。 (C) 2004 Elsevier Ltd. 保留所有权利。
The mechanisms that govern the ordered assembly of multiprotein ribonucleoprotein complexes are not well understood. The in vitro reconstitution of the small subunit of the bacterial ribosome provides a tractable system for the detailed study of ordered assembly. We present a quantitative thermodynamic description of the hierarchical binding of ribosomal proteins to 16 S rRNA during assembly of the platform of the 30 S ribosomal subunit. The binding of S8, S11, S15, and the S6:S18 heterodimer to the central domain of 16 S rRNA has been measured both individually and in combination using isothermal titration calorimetry and gel mobility shift assays. Both enthalpy and free energy measurements demonstrate the cooperative binding of S15 and the S6:S18 heterodimer, but no cooperativity is observed for either S8 or S11. The results define a thermodynamic framework that describes cooperative platform assembly. (C) 2004 Elsevier Ltd. All rights reserved.