Site-Specific Solid-State NMR Studies of "Trigger Factor" in Complex with the Large Ribosomal Subunit 50S
Site-Specific Solid-State NMR Studies of "Trigger Factor" in Complex with the Large Ribosomal Subunit 50S
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DOI：
10.1002/anie.201409393
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发表时间：
2015-03-27
影响因子：
16.6
通讯作者：
Reif, Bernd
中科院分区：
文献类型：
--
作者：
Barbet-Massin, Emeline;Huang, Chih-Ting;Reif, Bernd
尽管有高分辨率的核糖体晶体结构，但共翻译蛋白质折叠尚未得到很好的理解。我们提出了第一个固态核磁共振数据的非移动区域的原核核糖体复合物。局部化学位移扰动和线加宽观察到的骨架酰胺共振对应的触发因子核糖体结合结构域中的区域，参与与核糖体直接接触或经历构象变化后，核糖体结合。这种大的不对称蛋白质复合物（1.4 MDa）变得可访问的质子检测和高MAS频率（60 kHz）的结合使用的NMR调查。这些结果为理解大分子机器的机制提供了新的视角。
Co-translational protein folding is not yet well understood despite the availability of high-resolution ribosome crystal structures. We present first solid-state NMR data on non-mobile regions of a prokaryotic ribosomal complex. Localized chemical shift perturbations and line broadening are observed for the backbone amide resonances corresponding to the regions in the trigger factor ribosome-binding domain that are involved in direct contact with the ribosome or undergo conformational changes upon ribosome binding. This large asymmetric protein complex (1.4 MDa) becomes accessible for NMR investigations by the combined use of proton detection and high MAS frequencies (60 kHz). The presented results open new perspectives for the understanding of the mechanism of large molecular machineries.