Structure of ribonuclease P--a universal ribozyme.
Structure of ribonuclease P--a universal ribozyme.
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核糖核酸酶 P 的结构——通用核酶。
DOI：
10.1016/j.sbi.2006.04.002
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
Mondragon,Alfonso
中科院分区：
文献类型：
--
作者：
Torres-Larios,Alfredo;Swinger,KerrenK;Pan,Tao;Mondragon,Alfonso
核糖核酸酶P（Ribonuclease P，RNase P）是已知的两种通用核酶之一，也是最早被发现的核酶之一。它参与RNA加工，特别是tRNA的5′成熟。与大多数其他天然核酶不同，它以反式方式识别和切割其底物。RNase P是一种核糖核蛋白复合物，含有一个RNA亚基和少至一个蛋白质亚基。已经表明，在细菌和一些古细菌中，单独的RNA亚基可以支持催化作用。细菌RNase P RNA的结构和功能已被广泛研究，但详细的催化机制尚未完全了解。最近，已经描述了来自两种不同细菌的RNase P的结构域之一和整个RNA组分的结构。这些结构提供了关于RNA组分的结构组装以及参与底物识别和催化的区域的第一个原子级信息。这些结构的比较揭示了一个高度保守的核心，包括两个普遍保守的结构模块。有趣的是，相同的结构核心可以在不同的支架中找到。
Ribonuclease P (RNase P) is one of only two known universal ribozymes and was one of the first ribozymes to be discovered. It is involved in RNA processing, in particular the 5′ maturation of tRNA. Unlike most other natural ribozymes, it recognizes and cleaves its substrate in trans. RNase P is a ribonucleoprotein complex containing one RNA subunit and as few as one protein subunit. It has been shown that, in bacteria and in some archaea, the RNA subunit alone can support catalysis. The structure and function of bacterial RNase P RNA have been studied extensively, but the detailed catalytic mechanism is not yet fully understood. Recently, structures of one of the structural domains and of the entire RNA component of RNase P from two different bacteria have been described. These structures provide the first atomic-level information on the structural assembly of the RNA component, and the regions involved in substrate recognition and catalysis. Comparison of these structures reveals a highly conserved core that comprises two universally conserved structural modules. Interestingly, the same structural core can be found in the context of different scaffolds.