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Query: EC:3.1.13.1 (exoribonuclease)
 732 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A new ribonuclease has been isolated from Escherichia coli. The enzyme is present in the 100,000 times g supernatant fraction and has been purified over 200-fold. Studies of the enzyme reveal that: 1. The enzyme shows a marked preference for oligoribonucleotides; indeed, the reaction rate is inversely proportional to the chain length of the substrate. The enzyme does not attack polynucleotides even at high concentrations of enzyme and has no detectable DNase activity. 2. The enzyme is stimulated strongly by Mn2+, less strongly by Mg2+, and not at all by Ca2+ and monovalent cations. 3. The enzyme is purified free of RNase I, RNase II, RNase III, polynucleotide phosphorylase, and other known ribonucleases of E. coli. The enzyme displays identical properties when isolated from mutants of E. coli that are deficient in the above ribonucleases. 4. The enzyme has a marked thermostability, a point of further distinction from RNase II.
J Biol Chem 1975 Sep 25
PMID:A novel oligoribonuclease of Escherichia coli. I. Isolation and properties. 24 Aug 24

The exoribonuclease in bovine brain has been purified about 900-fold in 10% yield. The molecular weight is about 65,000. The enzyme is free from other ribonucleases of bovine brain. Studies of the mode of action of the enzyme show the following: (a) The enzyme cleaves both oligo- and polyribonucleotides exonucleolytically, initiating nucleolytic attack from the 5'-hydroxyl end to yield 3'-mononucleotides. The enzyme differs from spleen exonuclease in that it does not act on polydeoxyribonucleotides. (b) When the 5'-hydroxyl group is phosphorylated, the enzyme is inactive. (c) The enzymic action is processive in nature; the enzyme hydrolyzes one polynucleotide chain to completion before proceeding to the degradation of another chain.
J Biol Chem 1977 Sep 25
PMID:Purification and mode of action of exoribonuclease from bovine brain. 89 14

In a mutant strain defective in polynucleotide phosphorylase, under conditions where the enzyme becomes limiting, it is possible to demonstrate that chemical as well as functional half lives of mRNA become longer if the strain is also missing ribonuclease II. These results allow to unify in a simple model a variety of observations about turnover of RNA in a variety of bacteria.
Mol Gen Genet 1975 Sep 08
PMID:Polynucleotide phosphorylase can participate in decay of mRNA in Escherichia coli in the absence of ribonuclease II. 110 47

Two 3'-5' exoribonucleases, polynucleotide phosphorylase and ribonuclease II play a central role in the degradation of bacterial mRNA to ribonucleotides. Sequences with the potential to form stem-loop structures can stabilize upstream mRNA against 3'-5' exoribonucleolytic attack in vivo by blocking the processive activities of these enzymes. For many mRNA species stem-loop structures appear to provide a very efficient block to decay from the 3' end, such that the rate-determining step for mRNA decay occurs elsewhere in the transcript. We have examined the stalling of 3'-5' exoribonucleases at stem-loop structures in vitro. Although stem-loop structures alone can impede the progress of both enzymes, the duration of stalling at these structures in vitro is insufficient to account for the increased half-lives that they confer on mRNA in vivo. These data suggest that an additional factor, such as a stem-loop binding protein, is required for stabilization of mRNA by stem-loop structures in vivo. The implications for the regulation of mRNA stability are discussed.
J Mol Biol 1991 Sep 05
PMID:mRNA degradation by processive 3'-5' exoribonucleases in vitro and the implications for prokaryotic mRNA decay in vivo. 192 Apr 21

Because of evidence of an immunologic role for ribonuclease II (E.C. 3.1.27.5) in mammals, its presence in milk was further characterized to provide a basis for study of possible contributions of its activity to the health of infants. Isoenzymes of ribonuclease II were quantitatively resolved from milk samples as small as 1 ml or less by chromatography on phosphocellulose. Three isoenzymes detected in bovine milk were the previously reported ribonucleases A and B and a form termed ribonuclease II-1. These isoenzymes were in the ratio of 70:30:1. Form II-1 was unique in its inability to hydrolyze polycytidylate. Bovine colostrum contained 10 to 15 times more ribonuclease II-1 than does milk and three times more total ribonuclease II per unit volume. Human milk contains about 1% the concentration of ribonuclease II found in cows' milk. Ribonuclease II activity in milk was quite stable in the acidic conditions of whey production and during low heat treatments. However, most of its enzymatic activity was lost with high heat treatments. No commercially manufactured milk-based or soybean-based infant formula assayed contained nearly as much ribonuclease activity as either human or bovine milk.
J Dairy Sci 1987 Sep
PMID:Ribonuclease activity and isoenzymes in raw and processed cows' milk and infant formulas. 366 41

A mutant strain of Escherichia coli previously thought to possess low levels of ribonuclease II activity has normal levels of ribonuclease II after partial purification of this enzyme from crude extracts.
J Bacteriol 1972 Sep
PMID:Ribonuclease II activity in a "presumptive" ribonuclease II-deficient mutant. 455 34

1. Ribonuclease II of Escherichia coli degrades pulse-labelled RNA associated with ribosomes and polyuridylic acid on ribosomes and in solution to mononucleotides. 2. Ribosomal and pulse-labelled RNA in solution and ribosomal RNA in chloramphenicol particles (protein-deficient ribosomes) are degraded to oligonucleotides. 3. Ribosomal RNA in mature ribosomes is not attacked by the enzyme. 4. From the mode of action of ribonuclease II, which is specific for single-stranded polyribonucleotides and does not attack helical forms, it is inferred that pulse-labelled RNA associated with ribosomes of E. coli exists as a single-stranded structure and that ribosomal RNA in chloramphenicol particles has a pronounced helical character. 5. The different behaviour of ribonuclease II towards newly synthesized RNA, ribosomal RNA and chloramphenicol-particle RNA in E. coli ribosomes is discussed.
Biochem J 1967 Sep
PMID:The conformation of ribonucleic acids in Escherichia coli ribosomes. Inferences from the mode of action of ribonuclease II. 486 Jun 40

A single-strand-specific, nucleolar exoribonuclease from Ehrlich ascites tumor cells has been isolated and purified free from other nucleases. The exonuclease degraded single-stranded RNA processively from either a 5'-hydroxyl or a 5'-phosphorylated end and released 5'-mononucleotides. The enzyme digested single-strand poly(C), poly(U), and poly(A) equally well but did not degrade duplex poly(C).poly(I) or poly(A).poly(U). Less than 0.2% of duplex DNA or 1.5% of heat-denatured DNA was degraded under the conditions which resulted in greater than 26% degradation of RNA. The ribonuclease required Mg2+ (0.2 mM) for optimum activity and was inhibited by ethylenediaminetetraacetic acid but not by human placental RNase inhibitor. The native enzyme had a Stokes radius of 42 A and a sedimentation coefficient (S20,w) of 4.3 S. From these values, an apparent molecular weight of 76 000 was derived by using the Svedberg equation. The localization and unique mode of degradation suggest a role for the 5'----3' exoribonuclease in ribosomal RNA processing.
Biochemistry 1984 Sep 11
PMID:Isolation and properties of a single-strand 5'----3' exoribonuclease from Ehrlich ascites tumor cell nucleoli. 620 56

RNA-OUT, the 69-nucleotide antisense RNA that regulates Tn10/IS10 transposition folds into a simple stem-loop structure. The unusually high metabolic stability of RNA-OUT is dependent, in part, on the integrity of its stem-domain: mutations that disrupt stem-domain structure (Class II mutations) render RNA-OUT unstable, and restoration of structure restores stability. Indeed, there is a strong correlation between the thermodynamic and metabolic stabilities of RNA-OUT. We show here that stem-domain integrity determines RNA-OUT's resistance to 3' exoribonucleolytic attack: Class II mutations are almost completely suppressed in Escherichia coli cells lacking its principal 3' exoribonucleases, ribonuclease II (RNase II) and polynucleotide phosphorylase (PNPase). RNase II and PNPase are individually able to degrade various RNA-OUT species, albeit with different efficiencies: RNA-OUT secondary structure provides greater resistance to RNase II than to PNPase. Surprisingly, RNA-OUT is threefold more stable in wild-type cells than in cells deficient for RNase II activity, suggesting that RNase II somehow lessens PNPase attack on RNA-OUT. We discuss how this might occur. We also show that wild-type RNA-OUT stability changes only two-fold across the normal range of physiological growth temperatures (30-44 degrees C) in wild-type cells, which has important implications for IS10 biology.
Mol Microbiol 1994 Sep
PMID:Decay of the IS10 antisense RNA by 3' exoribonucleases: evidence that RNase II stabilizes RNA-OUT against PNPase attack. 753 7

Escherichia coli RNase E, an essential single-stranded specific endoribonuclease, is required for both ribosomal RNA processing and the rapid degradation of mRNA. The availability of the complete sequences of a number of bacterial genomes prompted us to assess the evolutionarily conservation of bacterial RNase E. We show here that the sequence of the N-terminal endoribonucleolytic domain of RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria. Furthermore, we demonstrate that the Synechocystis sp. homologue binds RNase E substrates and cleaves them at the same position as the E. coli enzyme. Taken together these results suggest that RNase E-mediated mechanisms of RNA decay are not confined to E. coli and its close relatives. We also show that the C-terminal half of E. coli RNase E is both sufficient and necessary for its physical interaction with the 3'-5' exoribonuclease polynucleotide phosphorylase, the RhlB helicase, and the glycolytic enzyme enolase, which are components of a "degradosome" complex. Interestingly, however, the sequence of the C-terminal half of E. coli RNase E is not highly conserved evolutionarily, suggesting diversity of RNase E interactions with other RNA decay components in different organisms. This notion is supported by our finding that the Synechocystis sp. RNase E homologue does not function as a platform for assembly of E. coli degradosome components.
Proc Natl Acad Sci U S A 1998 Sep 29
PMID:The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly. 975 18


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