Structural and functional similarities between MRP and RNase P.
RNase P, the enzyme response for 5'-end processing of tRNAs and 4.5S RNA, has been extensively characterized from E. coli. The RNA component of E. coli RNase P, without the protein, has the enzymatic activity and is the first true RNA enzyme to be characterized. RNase P and MRP are two distinct nuclear ribonucleoprotein (RNP) particles characterized in many eukaryotic cells including human, yeast and plant cells. There are many similarities between RNase P and MRP. These include: (1) sequence specific endonuclease activity; (2) homology at the primary and secondary structure levels; and (3) common proteins in both the RNPs. It is likely that RNase P and MRP originated from a common ancestor.
Department of Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA.
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D001483:Base Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D029968:Escherichia coli Proteins; D019143:Evolution, Molecular; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010944:Plants / Q000235:genetics; D016337:RNA, Catalytic / Q000737:chemistry* / Q000378:metabolism*; D043262:Ribonuclease P; D012261:Ribonucleoproteins / Q000737:chemistry / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D029968:Escherichia coli Proteins; D016337:RNA, Catalytic; D012261:Ribonucleoproteins; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; C468368:RPP14 protein, human; D043262:Ribonuclease P; C470865:ribonuclease P, E coli