RNase MRP and RNase P share a common substrate.
RNase MRP is a site-specific ribonucleoprotein endoribonuclease that processes RNA from the mammalian mitochondrial displacement loop containing region. RNase P is a site-specific ribonucleoprotein endoribonuclease that processes pre-tRNAs to generate their mature 5'-ends. A similar structure for the RNase P and RNase MRP RNAs and a common cleavage mechanism for RNase MRP and RNase P enzymes have been proposed. Experiments with protein synthesis antibiotics have shown that both RNase MRP and RNase P are inhibited by puromycin. We also show that E. coli RNase P cleaves the RNase MRP substrate, mouse mitochondrial primer RNA, exactly at a site that is cleaved by RNase MRP.
Potuschak
T
T
Institut für Tumorbiologie-Krebsforschung, Universität Wien, Austria.
Rossmanith
W
W
Karwan
R
R
D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D004722:Endoribonucleases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D051379:Mice; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011691:Puromycin / Q000494:pharmacology; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D016337:RNA, Catalytic / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000077278:RNA, Mitochondrial; D043262:Ribonuclease P; D013379:Substrate Specificity
D029968:Escherichia coli Proteins; D016337:RNA, Catalytic; D000077278:RNA, Mitochondrial; D011691:Puromycin; D012313:RNA; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; D043262:Ribonuclease P; C470865:ribonuclease P, E coli