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首页> 外文OA文献 >The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker
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The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker

机译：细菌翻译起始因子IF2的N端结构域（IF2N）通过柔性接头连接至保守的C端结构域

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摘要

Bacterial translation initiation factor IF2 is a multidomain protein that is an essential component of a system for ensuring that protein synthesis begins at the correct codon within a messenger RNA. Full-length IF2 from Escherichia coli and seven fragments of the protein were expressed, purified, and characterized using nuclear magnetic resonance (NMR) and circular dichroism (CD) methods. Interestingly, resonances of the 6 kD IF2N domain located at the extreme N terminus of IF2 can be clearly identified within the NMR spectra of the full-length 97-kD protein. 15N NMR relaxation rate data indicate that (1) the IF2N domain is internally well ordered and tumbles in solution in a manner that is independent of the other domains of the IF2 protein, and (2) the IF2N domain is connected to the C-terminal regions of IF2 by a flexible linker. Chemical shifts of resonances within the isolated IF2N domain do not significantly differ from those of the corresponding residues within the context of the full-length 97-kD protein, indicating that IF2N is a structurally independent unit that does not strongly interact with other regions of IF2. CD and NMR data together provide evidence that Domains I–III of IF2 have unstructured and flexible regions as well as substantial helical content; CD data indicate that the helical content of these regions decreases significantly at temperatures above 35°C. The features of structurally well-ordered N- and C-terminal domains connected by a flexible linker with significant helical content are reminiscent of another translation initiation factor, IF3.
机译：细菌翻译起始因子IF2是一种多域蛋白，是确保蛋白合成从信使RNA内的正确密码子开始的系统的重要组成部分。使用核磁共振（NMR）和圆二色性（CD）方法表达，纯化和鉴定了来自大肠杆菌的全长IF2和该蛋白的七个片段。有趣的是，可以在全长97-kD蛋白的NMR光谱中清楚地识别出位于IF2极端N末端的6 kD IF2N域的共振。 15N NMR弛豫速率数据表明（1）IF2N域内部有序排列并且在溶液中以不依赖IF2蛋白其他域的方式滚动，（2）IF2N域连接到C端IF2区域通过一个灵活的链接器。分离的IF2N域内的共振化学位移与全长97-kD蛋白上下文中相应残基的共振化学位移没有显着差异，表明IF2N是结构独立的单元，不会与IF2的其他区域强烈相互作用。 CD和NMR数据共同提供了证据，证明IF2的I-III结构域具有非结构化和灵活的区域以及大量的螺旋含量。 CD数据表明，这些区域的螺旋含量在高于35℃的温度下显着降低。由具有显着螺旋含量的柔性接头连接的结构良好有序的N和C末端结构域的特征使人联想到另一个翻译起始因子IF3。

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