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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >RNase P RNAs from some Archaea are catalytically active
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RNase P RNAs from some Archaea are catalytically active

机译：来自某些古细菌的RNase P RNA具有催化活性

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摘要

The RNA subunits of RNase Ps of Archaea and eukaryotes have been thought to depend fundamentally on protein for activity, unlike those of Bacteria that are capable of efficient catalysis in the absence of protein. Although the eukaryotic RNase P RNAs are quite different than those of Bacteria in both sequence and structure, the archaeal RNAs generally contain the sequences and structures of the bacterial, phylogenetically conserved catalytic core. A spectrum of archaeal RNase P RNAs were there fore tested for activity in a wide range of conditions. Many remain inactive in ionically extreme conditions, but catalytic activity could be detected from those of the methanobacteria, thermococci, and halobacteria. Chimeric holoenzymes, reconstituted from the Methanobacterium RNase P RNA and the Bacillus subtilis RNase P protein subunits, were functional at low ionic strength. The properties of the archaeal RNase P RNAs (highionic-strength requirement, low affinity for substrate, and catalytic reconstitution by bacterial RNase P protein) are sililar to synthetic RNase P RNAs that contain all of the catalytic core of the bacterial RNA but lack phylogenetically variable, stabilizing elements.
机译：人们认为古细菌和真核生物的RNase Ps的RNA亚基从根本上依赖于蛋白质的活性，这与不存在蛋白质的情况下能够有效催化的细菌不同。尽管真核RNase P RNA的序列和结构与细菌完全不同，但古细菌RNA通常包含细菌，系统发育上保守的催化核心的序列和结构。预先测试了一系列古细菌RNase P RNA在各种条件下的活性。许多在离子极端条件下仍然没有活性，但是可以从甲烷细菌，嗜热球菌和卤细菌的催化活性中检测到。嵌合全酶，由甲烷杆菌RNase P RNA和枯草芽孢杆菌RNase P蛋白亚基组成，在低离子强度下具有功能。古细菌RNase P RNA的特性（离子强度要求高，对底物的亲和力低以及细菌RNase P蛋白的催化重构）与合成RNase P RNA相似，后者包含细菌RNA的所有催化核心，但缺乏系统发育变量，稳定元素。

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