Fagerlund Robert D, Perederina Anna, Berezin Igor, Krasilnikov Andrey S
Department of Biochemistry and Molecular Biology, Center for RNA Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
RNA. 2015 Sep;21(9):1591-605. doi: 10.1261/rna.049007.114. Epub 2015 Jul 1.
Ribonuclease (RNase) P and RNase MRP are closely related catalytic ribonucleoproteins involved in the metabolism of a wide range of RNA molecules, including tRNA, rRNA, and some mRNAs. The catalytic RNA component of eukaryotic RNase P retains the core elements of the bacterial RNase P ribozyme; however, the peripheral RNA elements responsible for the stabilization of the global architecture are largely absent in the eukaryotic enzyme. At the same time, the protein makeup of eukaryotic RNase P is considerably more complex than that of the bacterial RNase P. RNase MRP, an essential and ubiquitous eukaryotic enzyme, has a structural organization resembling that of eukaryotic RNase P, and the two enzymes share most of their protein components. Here, we present the results of the analysis of interactions between the largest protein component of yeast RNases P/MRP, Pop1, and the RNA moieties of the enzymes, discuss structural implications of the results, and suggest that Pop1 plays the role of a scaffold for the stabilization of the global architecture of eukaryotic RNase P RNA, substituting for the network of RNA-RNA tertiary interactions that maintain the global RNA structure in bacterial RNase P.
核糖核酸酶（RNase）P和RNase MRP是密切相关的催化核糖核蛋白，参与多种RNA分子的代谢，包括tRNA、rRNA和一些mRNA。真核生物RNase P的催化RNA组分保留了细菌RNase P核酶的核心元件；然而，负责稳定整体结构的外围RNA元件在真核酶中基本不存在。同时，真核生物RNase P的蛋白质组成比细菌RNase P的要复杂得多。RNase MRP是一种必需且普遍存在的真核酶，其结构组织类似于真核生物RNase P，并且这两种酶共享大部分蛋白质组分。在此，我们展示了对酵母RNases P/MRP最大的蛋白质组分Pop1与酶的RNA部分之间相互作用的分析结果，讨论了结果的结构意义，并表明Pop1起到了稳定真核生物RNase P RNA整体结构的支架作用，替代了在细菌RNase P中维持整体RNA结构的RNA - RNA三级相互作用网络。
