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Nucleic Acids Research, 1993, Vol. 21, No. 14 3239-3243
© 1993

MOLECULAR BIOLOGY

RNase MRP and RNase P share a common substrate

Thomas Potuschak, Walter Rossmanith and Robert Karwan

Instftut für Tumorbiotogie-Krebsforschung der Universität Wien, Genexpression Borschkegasse 8a, A-1090 Wien, Austria

Received March 17, 1993. Revised June 8, 1993. Accepted June 8, 1993.

RNase MRP is a site-specific ribonucleoprotein endo ribonuclease that processes RNA from the mammalian mitochondrial displacement ioop containing region. RNase P is a site-specific ribonucleoprotein endoribo nuclease that processes pre-tRNAs to generate their mature 5'-ends. A similar structure for the RNase P and RNase MRP RNA5 and a common cleavage mechanism for RNase MRP and RNase P enzymes have been proposed. Experiments with protein synthesis anti biotics have shown that both RNase MAP and RNase P are inhibited by puromycin. We also show that E.coll RNase P cleaves the RNase MAP substrate, mouse mitochondrial primer RNA, exactiy at a site that is cleaved by RNase MRP.


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