Secondary structure probing of the human RNase MRP RNA reveals the potential for MRP RNA subsets.
RNase MRP is a ribonucleoprotein endoribonuclease involved in eukaryotic pre-rRNA processing. The enzyme possesses an RNA subunit, structurally related to that of RNase P RNA, that is thought to be catalytic. RNase MRP RNA sequences from Saccharomycetaceae species are structurally well defined through detailed phylogenetic and structural analysis. In contrast, higher eukaryote MRP RNA structure models are based on comparative sequence analysis of only five sequences and limited probing data. Detailed structural analysis of the Homo sapiens MRP RNA, entailing enzymatic and chemical probing, is reported. The data are consistent with the phylogenetic secondary structure model and demonstrate unequivocally that higher eukaryote MRP RNA structure differs significantly from that reported for Saccharomycetaceae species. Neither model can account for all of the known MRP RNAs and we thus propose the evolution of at least two subsets of RNase MRP secondary structure, differing predominantly in the predicted specificity domain.
Walker
Scott C
SC
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-0606, USA.
Avis
Johanna M
JM
D000465:Algorithms; D000818:Animals; D001483:Base Sequence; D002384:Catalysis; D004722:Endoribonucleases / Q000737:chemistry*; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010802:Phylogeny; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry*; D004718:Saccharomycetales / Q000235:genetics* / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D013379:Substrate Specificity; D014158:Transcription, Genetic
D012313:RNA; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease