Secondary structure of RNase MRP RNA as predicted by phylogenetic comparison.
RNase MRP is a ribonucleoprotein endoribonuclease that has been shown to cleave mitochondrial primer RNA sequences from a variety of sources. The bulk of RNase MRP activity is found in the nucleus where its function remains unknown. Two different approaches have resulted in predictions of distinct secondary structures for RNase MRP RNA. In order to analyze more definitively the higher-order structure of RNase MRP RNA, we have conducted a phylogenetic comparison of the available RNase MRP RNA sequences from human, mouse, rat, cow, toad, and yeast. The resulting secondary structure shares features in common with previously described structures for prokaryotic and eukaryotic RNase P RNAs (1) and RNase MRP RNAs (2, 3). In addition, the phylogenetic structure is consistent with available chemical modification data on RNase MRP RNA and with the detailed analysis of the To antigen binding domain located near the 5' end of the RNase MRP RNA. The structure is not limited to RNase MRP RNAs, but can be expanded to cover both eukaryotic RNase P RNAs and RNase P/MRP RNAs from plants.
Schmitt
M E
ME
Department of Developmental Biology, Stanford University School of Medicine, California 94305-5427.
Bennett
J L
JL
Dairaghi
D J
DJ
Clayton
D A
DA
D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D004722:Endoribonucleases / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D008928:Mitochondria / Q000737:chemistry*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010802:Phylogeny; D012329:RNA, Bacterial / Q000737:chemistry; D016337:RNA, Catalytic / Q000737:chemistry; D043262:Ribonuclease P; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D012329:RNA, Bacterial; D016337:RNA, Catalytic; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; C468368:RPP14 protein, human; D043262:Ribonuclease P