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. 1993 Jul 11;21(14):3239–3243. doi: 10.1093/nar/21.14.3239

RNase MRP and RNase P share a common substrate.

T Potuschak 1, W Rossmanith 1, R Karwan 1
PMCID: PMC309761  PMID: 7688115

Abstract

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.

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Selected References

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