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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure of Pfu Pop5, an archaeal RNase P protein
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Structure of Pfu Pop5, an archaeal RNase P protein

机译：Pfu Pop5（一种古细菌RNase P蛋白）的结构

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摘要

We have used NMR spectroscopy and x-ray crystallography to determine the three-dimensional structure of PF1378 (Pfu Pop5), one of four protein subunits of archaeal RNase P that shares a homolog in the eukaryotic enzyme. RNase P is an essential and ubiquitous ribonucleoprotein enzyme required for maturation of tRNA. In bacteria, the enzyme's RNA subunit is responsible for cleaving the single-stranded 5' leader sequence of precursor tRNA molecules (pre-tRNA), whereas the protein subunit assists in substrate binding. Although in bacteria the RNase P holoenzyme consists of one large catalytic RNA and one small protein subunit, in archaea and eukarya the enzyme contains several ( ≥ 4) protein subunits, each of which lacks sequence similarity to the bacterial protein. The functional role of the proteins is poorly understood, as is the increased complexity in comparison to the bacterial enzyme. Pfu Pop5 has been directly implicated in catalysis by the observation that it pairs with PF1914 (Pfu Rpp30) to functionally reconstitute the catalytic domain of the RNA subunit. The protein adopts an α-β sandwich fold highly homologous to the single-stranded RNA binding RRM domain. Furthermore, the three-dimensional arrangement of Pfu Pop5's structural elements is remarkably similar to that of the bacterial protein subunit. NMR spectra have been used to map the interaction of Pop5 with Pfu Rpp30. The data presented permit tantalizing hypotheses regarding the role of this protein subunit shared by archaeal and eukaryotic RNase P.
机译：我们已经使用NMR光谱学和X射线晶体学来确定PF1378（Pfu Pop5）的三维结构，PF1378是古细菌RNase P的四个蛋白质亚单位之一，在真核酶中具有同源性。 RNase P是tRNA成熟所需的必需且普遍存在的核糖核糖核酸酶。在细菌中，酶的RNA亚基负责切割前体tRNA分子（pre-tRNA）的单链5'前导序列，而蛋白质亚基则有助于底物结合。尽管在细菌中，RNase P全酶由一个大的催化RNA和一个小蛋白亚基组成，但在古细菌和真核生物中，该酶包含几个（≥4个）蛋白亚基，每个蛋白亚基都与细菌蛋白缺乏序列相似性。人们对蛋白质的功能作用了解甚少，与细菌酶相比，其复杂性也在增加。通过观察到Pfu Pop5与PF1914（Pfu Rpp30）配对，可以在功能上重构RNA亚基的催化结构域，从而直接参与了催化。该蛋白质采用与单链RNA结合RRM结构域高度同源的α-β三明治折叠。此外，Pfu Pop5的结构元件的三维排列与细菌蛋白亚基的排列非常相似。 NMR光谱已用于绘制Pop5与Pfu Rpp30的相互作用。所提供的数据令人陶醉地提出了关于古细菌和真核RNase P共有的这种蛋白质亚基的作用的假说。

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