RNase MRP and RNase P Share a Common Substrate

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1993 Jul 11

PMID 7688115

Citations 17

Authors

T Potuschak

W Rossmanith

R Karwan

Affiliations

Soon will be listed here.

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.

Citing Articles

Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components.

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Broadening the mission of an RNA enzyme.

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3D model of RNA polymerase and bidirectional transcription.

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Kinetics of inhibition of ribonuclease P activity by peptidyltransferase inhibitors. Effect of antibiotics on RNase P.

Kalavrizioti D, Vourekas A, Tekos A, Tsagla A, Stathopoulos C, Drainas D Mol Biol Rep. 2003; 30(1):9-14.

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Effect of peptidyltransferase inhibitors on ribonuclease P activity from Dictyostelium discoideum. Effect of antibiotics on RNase P.

Stathopoulos C, Tsagla A, Tekos A, Drainas D Mol Biol Rep. 2000; 27(2):107-11.

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