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与延伸因子-Tu结合到核糖体相关的运动中心。

Centers of motion associated with EF-Tu binding to the ribosome.

作者信息

Paci Maxim, Fox George E

机构信息

a Department of Biology and Biochemistry , University of Houston , Houston , TX , USA.

出版信息

RNA Biol. 2016 May 3;13(5):524-30. doi: 10.1080/15476286.2015.1114204. Epub 2016 Jan 19.

Abstract

Structural centers of motion (pivot points) in the ribosome have recently been identified by measurement of conformational changes in rRNA resulting from EF-G GTP hydrolysis. This series of measurements is extended here to the ribosome's interactions with the cofactor EF-Tu. Four recent EF-Tu bound ribosome structures were compared to unbound structures. A total of 16 pivots were identified, of which 4 are unique to the EF-Tu interaction. Pivots in the GTPase associated center and the sarcin-ricin loop omitted previously, are found to be mobile in response to both EF-Tu and EF-G binding. Pivots in the intersubunit bridge rRNAs are found to be cofactor specific. Head swiveling motions in the small subunit are observed in the EF-Tu bound structures that were trapped post GTP hydrolysis. As in the case of pivots associated with EF-G, the additional pivots described here are associated with weak points in the rRNA structures such as non-canonical pairs and bulge loops. The combined set of pivots should be regarded as a minimal set. Only several states available to the ribosome have been presented in this work. Future, precise crystal structures in conjunction with experimental data will likely show additional functional pivoting elements in the rRNA.

摘要

核糖体中的结构运动中心(枢轴点)最近已通过测量EF-G GTP水解导致的rRNA构象变化得以确定。在此,这一系列测量扩展至核糖体与辅因子EF-Tu的相互作用。将最近的四个结合了EF-Tu的核糖体结构与未结合的结构进行了比较。总共确定了16个枢轴点,其中4个是EF-Tu相互作用所特有的。先前遗漏的GTP酶相关中心和肌动蛋白-蓖麻毒素环中的枢轴点,被发现会因EF-Tu和EF-G的结合而发生移动。亚基间桥rRNA中的枢轴点具有辅因子特异性。在GTP水解后捕获的结合了EF-Tu的结构中,观察到小亚基中的头部旋转运动。与EF-G相关的枢轴点情况一样,此处描述的额外枢轴点与rRNA结构中的弱点相关,如非规范碱基对和凸起环。这组枢轴点应被视为一个最小集合。这项工作仅展示了核糖体可呈现的几种状态。未来,精确的晶体结构结合实验数据可能会显示rRNA中更多的功能性枢转元件。

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