Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.8 (polynucleotide phosphorylase)
 723 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Oligoribonuclease, an exoribonuclease specific for small oligoribonucleotides, was initially characterized 20 years ago (S. K. Niyogi and A. K. Datta, J. Biol. Chem. 250:7307-7312, 1975) and shown to be different from RNase II and polynucleotide phosphorylase. Here we demonstrate, using mutant strains and purified enzymes, that oligoribonuclease is not a manifestation of RNases D, BN, T, PH, and R, exoribonucleases discovered subsequently. Thus, oligoribonuclease is the eighth distinct exoribonuclease discovered in Escherichia coli. We also show that oligoribonuclease copurifies with polynucleotide phosphorylase.
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PMID:Oligoribonuclease is distinct from the other known exoribonucleases of Escherichia coli. 760 90

mRNA decay in prokaryotic cells involves the action of both endo- and exoribonucleases. In Escherichia coli, degradation of RNA to the mononucleotide level was thought to depend on RNase II and polynucleotide phosphorylase. Here, we show that the enzyme oligoribonuclease is an essential part of this process as well. Thus, inactivation of the orn gene encoding oligoribonuclease leads to a cessation of cell growth. Moreover, although pulse-labeled RNA decays normally in orn mutant cells under nonpermissive conditions, a large fraction of the resulting products is small oligoribonucleotides rather than the mononucleotides generated in wild-type cells. The oligoribonucleotides that accumulate are 2-5 residues in length; longer molecules disappear during the decay process. These data indicate that oligoribonuclease is required to complete the degradation of mRNA to mononucleotides and that this process is required for cell viability. Inasmuch as close homologues of the orn gene are found in a wide range of eukaryotes, extending up to humans, these findings raise the possibility that oligoribonuclease also participates in mRNA degradation in these organisms.
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PMID:Oligoribonuclease is an essential component of the mRNA decay pathway. 1020 Feb 69

RNA degradation is a major process controlling RNA levels and plays a central role in cell metabolism. From the labile messenger RNA to the more stable noncoding RNAs (mostly rRNA and tRNA, but also the expanding class of small regulatory RNAs) all molecules are eventually degraded. Elimination of superfluous transcripts includes RNAs whose expression is no longer required, but also the removal of defective RNAs. Consequently, RNA degradation is an inherent step in RNA quality control mechanisms. Furthermore, it contributes to the recycling of the nucleotide pool in the cell. Escherichia coli has eight 3'-5' exoribonucleases, which are involved in multiple RNA metabolic pathways. However, only four exoribonucleases appear to accomplish all RNA degradative activities: polynucleotide phosphorylase (PNPase), ribonuclease II (RNase II), RNase R, and oligoribonuclease. Here, we summarize the available information on the role of bacterial 3'-5' exoribonucleases in the degradation of different substrates, highlighting the most recent data that have contributed to the understanding of the diverse modes of operation of these degradative enzymes.
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PMID:The role of 3'-5' exoribonucleases in RNA degradation. 1921 73

This review provides a description of the known Escherichia coli ribonucleases (RNases), focusing on their structures, catalytic properties, genes, physiological roles, and possible regulation. Currently, eight E. coli exoribonucleases are known. These are RNases II, R, D, T, PH, BN, polynucleotide phosphorylase (PNPase), and oligoribonuclease (ORNase). Based on sequence analysis and catalytic properties, the eight exoribonucleases have been grouped into four families. These are the RNR family, including RNase II and RNase R; the DEDD family, including RNase D, RNase T, and ORNase; the RBN family, consisting of RNase BN; and the PDX family, including PNPase and RNase PH. Seven well-characterized endoribonucleases are known in E. coli. These are RNases I, III, P, E, G, HI, and HII. Homologues to most of these enzymes are also present in Salmonella. Most of the endoribonucleases cleave RNA in the presence of divalent cations, producing fragments with 3'-hydroxyl and 5'-phosphate termini. RNase H selectively hydrolyzes the RNA strand of RNA?DNA hybrids. Members of the RNase H family are widely distributed among prokaryotic and eukaryotic organisms in three distinct lineages, RNases HI, HII, and HIII. It is likely that E. coli contains additional endoribonucleases that have not yet been characterized. First of all, endonucleolytic activities are needed for certain known processes that cannot be attributed to any of the known enzymes. Second, homologues of known endoribonucleases are present in E. coli. Third, endonucleolytic activities have been observed in cell extracts that have different properties from known enzymes.
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PMID:Exoribonucleases and Endoribonucleases. 2644 51

RNA decay is a key element of mitochondrial RNA metabolism. To date, the only well-documented machinery that plays a role in mtRNA decay in humans is the complex of polynucleotide phosphorylase (PNPase) and SUV3 helicase, forming the degradosome. REXO2, a homolog of prokaryotic oligoribonucleases present in humans both in mitochondria and the cytoplasm, was earlier shown to be crucial for maintaining mitochondrial homeostasis, but its function in mitochondria has not been fully elucidated. In the present study, we created a cellular model that enables the clear dissection of mitochondrial and non-mitochondrial functions of human REXO2. We identified a novel mitochondrial short RNA, referred to as ncH2, that massively accumulated upon REXO2 silencing. ncH2 degradation occurred independently of the mitochondrial degradosome, strongly supporting the hypothesis that ncH2 is a primary substrate of REXO2. We also investigated the global impact of REXO2 depletion on mtRNA, revealing the importance of the protein for maintaining low steady-state levels of mitochondrial antisense transcripts and double-stranded RNA. Our detailed biochemical and structural studies provide evidence of sequence specificity of the REXO2 oligoribonuclease. We postulate that REXO2 plays dual roles in human mitochondria, 'scavenging' nanoRNAs that are produced by the degradosome and clearing short RNAs that are generated by RNA processing.
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PMID:Human REXO2 controls short mitochondrial RNAs generated by mtRNA processing and decay machinery to prevent accumulation of double-stranded RNA. 3236 87