Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20.
Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20.
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DOI：
10.1016/j.jmb.2009.07.032
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发表时间：
2009-09-25
影响因子：
5.6
通讯作者：
Woodson, Sarah A.
中科院分区：
文献类型：
--
作者：
Ramaswamy, Priya;Woodson, Sarah A.
核糖体蛋白稳定rRNA的折叠结构，并使更多的蛋白质能够募集到复合物中。定量羟基自由基足迹法用于测量三种不同的初级组装蛋白S4、S17和S20稳定E. coli16S5 ′结构域。络合物的稳定性受到扰动，通过改变氯化镁的浓度。每种蛋白质都影响rRNA三级相互作用的稳定性，超出其直接结合位点。S4和S17稳定整个5′结构域，而S20具有更局部的作用。5′结构域内单个螺旋的多阶段折叠表明，每种蛋白质稳定了不同的结构中间体体系，包括低Mg2+下的非天然相互作用。我们建议，S4，S17和S20与不同的螺旋连接的组合相互作用偏向自由能景观向几个RNA构象，有能力添加二级组装蛋白S16在下一步的组装。
Ribosomal proteins stabilize the folded structure of the rRNA and enable the recruitment of further proteins to the complex. Quantitative hydroxyl radical footprinting was used to measure the extent to which three different primary assembly proteins, S4, S17 and S20, stabilize the 3D structure of the E. coli 16S 5′ domain. The stability of the complexes was perturbed by varying the concentration of MgCl2. Each protein influences the stability of the rRNA tertiary interactions beyond its immediate binding site. S4 and S17 stabilize the entire 5′ domain, while S20 has a more local effect. Multi-stage folding of individual helices within the 5′ domain shows that each protein stabilizes a different ensemble of structural intermediates, that include non-native interactions at low Mg2+. We propose that the combined interactions of S4, S17 and S20 with different helical junctions bias the free energy landscape toward a few RNA conformations that are competent to add the secondary assembly protein S16 in the next step of assembly.
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