Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components

被引:17
作者
Fagerlund, Robert D. [1 ]
Perederina, Anna [1 ]
Berezin, Igor [1 ]
Krasilnikov, Andrey S. [1 ]
机构
[1] Penn State Univ, Dept Biochem & Mol Biol, Ctr RNA Mol Biol, University Pk, PA 16802 USA
基金
美国国家卫生研究院;
关键词
RNase P; RNase MRP; Pop1; ribonucleoprotein; RNA folding; Saccharomyces cerevisiae; PRECURSOR RIBOSOMAL-RNA; CELL-CYCLE PROGRESSION; RIBONUCLEASE-P; CRYSTAL-STRUCTURE; MRP RNA; MITOCHONDRIAL; SUBUNITS; DOMAIN; IDENTIFICATION; COMPLEX;
D O I
10.1261/rna.049007.114
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1591 / 1605
页数:15
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