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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural insights into the assembly of the human and archaeal signal recognition particles.
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Structural insights into the assembly of the human and archaeal signal recognition particles.

机译：结构洞察人类的组装和古细菌信号识别颗粒。

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摘要

The signal recognition particle (SRP) is a conserved ribonucleoprotein (RNP) complex that co-translationally targets membrane and secretory proteins to membranes. The assembly of the particle depends on the proper folding of the SRP RNA, which in mammalia and archaea involves an induced-fit mechanism within helices 6 and 8 in the S domain of SRP. The two helices are juxtaposed and clamped together upon binding of the SRP19 protein to their apices. In the current assembly paradigm, archaeal SRP19 causes the asymmetric loop of helix 8 to bulge out and expose the binding platform for the key player SRP54. Based on a heterologous archaeal SRP19-human SRP RNA structure, mammalian SRP19 was thought not to be able to induce this change, thus explaining the different requirements of SRP19 for SRP54 recruitment. In contrast, the crystal structures of a crenarchaeal and the all-human SRP19-SRP RNA binary complexes presented here show that the asymmetric loop is bulged out in both binary complexes. Differences in SRP assembly between mammalia and archaea are therefore independent of SRP19 and are based on differences in SRP RNA itself. A new SRP-assembly scheme is presented.
机译：信号识别粒子(SRP)守恒的核糖核蛋白(RNP)复杂co-translationally目标膜和分泌蛋白质膜。粒子取决于SRP的正确折叠在哺乳类和古生菌涉及一个RNA诱导契合机制在螺旋6和8SRP的S域。并列,对绑定的夹在一起SRP19蛋白到极点。组装模式,古SRP19导致不对称的螺旋循环8和突出暴露的绑定平台的关键球员SRP54。被认为不能够引起这种变化,因此解释的不同需求SRP19 SRP54招聘。crenarchaeal和晶体结构所有人类SRP19-SRP RNA二元复合物这里介绍表明,非对称循环二元复合物凸出来。在组装哺乳类与SRP古生菌因此SRP19和基于独立的SRP RNA本身的差异。提出了方案。

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