Conserved and variable domains of RNase MRP RNA

被引:41
作者
Lopez, Marcela Davila [1 ]
Rosenblad, Magnus Alm [2 ]
Samuelsson, Tore [1 ]
机构
[1] Univ Gothenburg, Inst Biomed, Sahlgrenska Acad, Dept Med Biochem & Cell Biol, SE-40530 Gothenburg, Sweden
[2] Univ Gothenburg, Dept Cell & Mol Biol, SE-40530 Gothenburg, Sweden
关键词
MRP; RNA; RNase MRP; RNase P; rRNA processing; K-turn; bioinformatics; CARTILAGE-HAIR HYPOPLASIA; PRE-RIBOSOMAL-RNA; CELL-CYCLE PROGRESSION; NUCLEOLAR; 7-2; RNA; RIBONUCLEASE-P; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; SECONDARY STRUCTURE; RMRP MUTATIONS; COMPUTATIONAL SCREEN;
D O I
10.4161/rna.6.3.8584
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 MRP is a eukaryotic ribonucleoprotein complex consisting of one RNA molecule and 7-10 protein subunits. One important function of MRP is to catalyze an endonucleolytic cleavage during processing of rRNA precursors. RNase MRP is evolutionary related to RNase P which is critical for tRNA processing. A large number of MRP RNA sequences that now are available have been used to identify conserved primary and secondary structure features of the molecule. MRP RNA has structural features in common with P RNA such as a conserved catalytic core, but it also has unique features and is characterized by a domain highly variable between species. Information regarding primary and secondary structure features is of interest not only in basic studies of the function of MRP RNA, but also because mutations in the RNA give rise to human genetic diseases such as cartilage-hair hypoplasia.
引用
收藏
页码:208 / 221
页数:14
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