Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.1 (RNase)
 16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A system consisting of 40-80S messenger ribonucleoprotein particles (mRNP) from stationary Friend erythroleukemia (FEL) cells was used to investigate the stability of mRNA in vitro. The majority of mRNP mRNAs were found to be stable when incubated for periods of up to ninety minutes at 37 degrees. Nonetheless, many mRNAs are greatly reduced in abundance, including ones for eucaryotic elongation factor Tu (eEF-Tu) and the 73-78 kDa polypeptide commonly found in association with the poly(A) tails of mRNA. A divalent cation dependent ribonuclease (probably an endoribonuclease) could be washed off mRNP by treatment of the particles with 0.5M NaCl. The mRNAs contained in the resultant salt washed mRNPs, including eEF-Tu, were stable when incubated in vitro.
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PMID:An in vitro system derived from Friend erythroleukemia cells to study messenger RNA stability. 347 22

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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PMID:The yeast, Saccharomyces cerevisiae, RNase P/MRP ribonucleoprotein endoribonuclease family. 890 93