Structure and mechanical properties of the ribosomal L1 stalk three-way junction.

Structure and mechanical properties of the ribosomal L1 stalk three-way junction.
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DOI:
10.1093/nar/gks258
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发表时间:
2012-07
影响因子:
14.9
通讯作者:
Lankas F
Lankas F
中科院分区:
生物学2区
文献类型:
--
作者:
Réblová K;Sponer J;Lankas F

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L1 茎是大核糖体亚基的关键移动元件,在易位过程中与 tRNA 相互作用。在这里,我们研究了来自四种不同原核生物的 L1 茎基部 rRNA H76/H75/H79 三路连接的结构和机械特性。我们提出了一个粗粒度弹性模型,并使用大规模原子分子动力学模拟对其进行参数化。连接的整体特性可以通过一个模型得到很好的描述,其中 H76 螺旋由直的各向同性柔性弹性杆表示,而连接核心由各向同性柔性球形铰链表示。核心和螺旋线对整体 H76 弯曲波动都有很大贡献。 H76 中摆动对的存在不会导致螺旋的任何灵活性或各向异性增加。 L1 柄的半封闭构象似乎可以通过连接本身的热波动来实现,而没有任何长程变构效应。 H76 的弯曲波动及其中引入的凸起表明了真核生物中凸起的精确位置的基本原理。我们的弹性模型可以推广到生物系统或纳米技术中发现的其他 RNA 连接。
The L1 stalk is a key mobile element of the large ribosomal subunit which interacts with tRNA during translocation. Here, we investigate the structure and mechanical properties of the rRNA H76/H75/H79 three-way junction at the base of the L1 stalk from four different prokaryotic organisms. We propose a coarse-grained elastic model and parameterize it using large-scale atomistic molecular dynamics simulations. Global properties of the junction are well described by a model in which the H76 helix is represented by a straight, isotropically flexible elastic rod, while the junction core is represented by an isotropically flexible spherical hinge. Both the core and the helix contribute substantially to the overall H76 bending fluctuations. The presence of wobble pairs in H76 does not induce any increased flexibility or anisotropy to the helix. The half-closed conformation of the L1 stalk seems to be accessible by thermal fluctuations of the junction itself, without any long-range allosteric effects. Bending fluctuations of H76 with a bulge introduced in it suggest a rationale for the precise position of the bulge in eukaryotes. Our elastic model can be generalized to other RNA junctions found in biological systems or in nanotechnology.
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