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首页> 外文期刊>Journal of Molecular Biology >The structure of RNA-free Rho termination factor indicates a dynamic mechanism of transcript capture.
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The structure of RNA-free Rho termination factor indicates a dynamic mechanism of transcript capture.

机译：无RNA的Rho终止因子的结构表明转录物捕获的动态机制。

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摘要

The Rho factor is a ring-shaped ATP-dependent helicase that mediates transcription termination in most prokaryotic cells by disengaging the transcription elongation complex formed by the RNA polymerase, DNA, and the nascent RNA transcript. The crystal structures of key intermediates along the kinetic pathway of RNA binding to Rho unveiled an unprecedented mode of helicase loading and provided a model for the ATP turnover coupled to coordinated strand movement. Here we report the structure of the early RNA-free state of Rho, which had eluded crystallization for many years but now completes the series. The structure allows the characterization of the apo-form Rho from Thermotoga maritima to 2.3 A resolution, reveals an RNA-recruiting site that becomes hidden after occupancy of the adjacent specific primary RNA-binding site, and suggests an enriched model for mRNA capture that is consistent with previous data.
机译：Rho因子是一种环形的ATP依赖性解旋酶，可通过解离由RNA聚合酶，DNA和新生RNA转录物形成的转录延伸复合物来介导大多数原核细胞中的转录终止。沿着与Rho结合的RNA动力学路径，关键中间体的晶体结构揭示了一种前所未有的解旋酶加载模式，并为与协调链运动耦合的ATP转换提供了模型。在这里，我们报告了Rho的早期无RNA状态的结构，该状态已经结晶多年了，但是现在完成了该系列。该结构可以表征来自栖热菌（Thermotoga maritima）的载脂蛋白Rho到2.3 A的分辨率，揭示了一个RNA募集位点，该位点在相邻特定一级RNA结合位点被占据后就隐藏了，并提出了一个丰富的mRNA捕获模型。与以前的数据一致。

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