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The yeast,Saccharomyces cerevisiae, RNase P/MRP ribonucleoprotein endoribonuclease family

  • Special Issue: RNase MRP/RNase P Systems
  • RNase MRP
  • Published:
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Abstract

Ribonuclease P (RNase P) is a ribonucleoprotein responsible for the endonucleolytic cleavage of the 5′-termini of tRNAs. Ribonuclease MRP (RNase MRP) is a ribonucleoprotein that has the ability to cleave both mitochondrial RNA primers presumed to be involved in mitochondrial DNA replication and rRNA precursors for the production of mature rRNAs. Several lines of evidence suggest that these two ribonucleoproteins are related to each other, both functionally and evolutionarily. Both of these enzymes have activity in the nucleus and mitochondria. Each cleave their RNA substrates in a divalent cation dependent manner to generate 5′-phosphate and 3′-OH termini. In addition, the RNA subunits of both complexes can be folded into a similar secondary structure. Each can be immunoprecipitated from mammalian cells with Th antibodies. In yeast, both have been found to share at least one common protein. This review will discuss some of the recent advances in our understanding of the structure, function and evolutionary relationship of these two enzymes in the yeast,Saccharomyces cerevisiae.

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Abbreviations

LRI:

long range interaction

mt:

mitochondrial

MRP:

mitochondrial RNA processing

NME:

nuclear mitochondrial endonuclease

POP:

processing of precursor

RNase:

ribonuclease

SNM:

suppressor of NME

RNP:

ribonucleoprotein

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, SUNY Health Science Center at Syracuse, 750 East Adams Street, 13210, Syracuse, NY, USA

    Tracey H. Reilly & Mark E. Schmitt

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  1. Tracey H. Reilly
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  2. Mark E. Schmitt
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Reilly, T.H., Schmitt, M.E. The yeast,Saccharomyces cerevisiae, RNase P/MRP ribonucleoprotein endoribonuclease family. Mol Biol Rep 22, 87–93 (1995). https://doi.org/10.1007/BF00988711

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