Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.7.6 (RNA polymerase)
34,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Deoxyadenylylguanosine (dAdG, 0.2-0.4 mM), affecting the RNA polymerase activity, caused inhibition of transcription of the influenza A virus in presence of precursor AdG by 50-60% and a 80-85% inhibition in absence of the precursor. The inhibitor exhibited its effect independently on the time of addition into an incubation mixture. Addition of 0.5 mM inhibitor into a cultural medium inhibited reproduction of the influenza A virus in a culture of chicken embryonal fibroblasts.
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PMID:[Inhibitory effect of deoxyadenylyl-(3'-5')-deoxyguanosine on the RNA-polymerase activity of influenza virus A]. 409 Mar 58

Ten ribonucleic acid (RNA) tumor viruses grown in five different host cell species and three non-oncogenic viruses from three different virus groups have been examined for ribonuclease H content. Three different substrates were used to assay ribonuclease H: calf thymus [(3)H]RNA-deoxyribonucleic acid (DNA) hybrid prepared with denatured calf thymus DNA and Escherichia coli DNA-directed RNA polymerase, (3)H-polydenylic acid [(3)H-poly(A)] complexed to polydeoxythymidylic acid [poly(dT)], and (3)H-polyuridylic acid [(3)H-poly(U)] complexed to polydeoxyadenylic acid [poly(dA)]. All ten RNA tumor viruses contained ribonuclease H activity which degraded the RNA of both the calf thymus hybrid and poly(A)-poly(dT), whereas only the ribonuclease H in the Moloney strain of murine sarcoma-leukemia virus and in RD-feline leukemia virus hydrolyzed the RNA strand of poly(U)-poly(dA). No appreciable ribonuclease H activity was detected in influenza, Sendai, or vesicular stomatitis virus. The ribonuclease H and RNA-directed DNA polymerase activities in Moloney murine sarcoma-leukemia virus were inseparable by phosphocellulose chromatography or glycerol gradient centrifugation, but appeared to be partially separated by diethylaminoethyl-cellulose chromatography.
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PMID:Ribonuclease H: a ubiquitous activity in virions of ribonucleic acid tumor viruses. 411 67

Structures with RNA polymerase activity were isolated from influenza virus-infected cells, and consisted of ribonucleoprotein (RNP) complexes, similar in morphology to the viral internal component or nucleocapsid. The isolation procedure involved fractionation of infected cells in a discontinuous sucrose gradient, in which enzyme activity was concentrated in a fraction of intermediate density which contains both smooth and rough cytoplasmic membranes. The RNPs with polymerase activity were further purified in a velocity gradient, after which the peak fractions showed a 35-fold purification of the polymerase activity when compared with cytoplasmic extracts. The NP polypeptide, which is the subunit of the virion RNP, was the only virus-specific polypeptide detected in these RNP structures.
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PMID:Isolation and properties of an RNA polymerase from influenza virus-infected cells. 412 Jun 39

In vitro reaction conditions have been determined for the maximal synthesis of product ribonucleic acid by the influenza (WSN) virion ribonucleic acid polymerase. The reaction requires the presence of all four triphosphates, Mg(2+) and Mn(2+) ions, monovalent cations, nonionic detergent, and ribonucleoside triphosphates at concentrations above certain threshold values. The optimum pH for the reaction is around 8.0 to 8.2 and the kinetics of product synthesis are linear through at least 6 hr when incubated at 31 to 33 C.
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PMID:Transcription of the influenza ribonucleic acid genome by a virion polymerase. I. Optimal conditions for in vitro activity of the ribonucleic acid-dependent ribonucleic acid polymerase. 432 17

Nuclei purified from chicken embryo fibroblast cells infected with influenza (fowl plague) virus contain an RNA-dependent RNA polymerase. The in vitro activity of this enzyme is insensitive to actinomycin D, and is completely destroyed by preincubation with ribonuclease. Enzyme induction is prevented if cells are treated with actinomycin D or cycloheximide at the time of infection. RNA-dependent RNA polymerase activity increases rapidly in cell nuclei from 1 h postinfection, reaches a maximum at 3 to 4 h, then declines; a similar RNA polymerase activity in the microsomal cell fraction increases from 2 h postinfection and reaches a maximum at 5 to 6 h. The characteristics of the nuclear and microsomal enzymes in vitro are similar with respect to pH and divalent cation requirements. The in vitro products of enzyme activity present in the nuclear and microsomal fractions of cells infected for 3 and 5 h were characterized by sucrose density gradient analysis, and annealing to virion RNA. The microsomal RNA polymerase product contained 67 and 93% RNA complementary to virion RNA at 3 and 5 h, respectively; for the nuclear RNA polymerase product these values were 40% in each case.
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PMID:RNA-dependent RNA polymerase in nuclei of cells infected with influenza virus. 435 67

The replication of influenza virus in chick embryo fibroblast cells is inhibited by alpha-amanitin added during the first 2 hr of infection at concentrations similar to those required to inhibit cellular DNA-dependent RNA polymerase form II in vivo. Of two periods of increased RNA synthesis observed in cells infected with influenza virus, only the first, occurring from 0 to 2 hr after infection, is sensitive to alpha-amanitin. During this early period, there is a stimulation of the activity of DNA-dependent RNA polymerase II of nuclei isolated from infected cells. The data suggest that DNA transcription mediated by polymerase II is essential for influenza virus replication.
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PMID:Inhibition of influenza virus replication by -amanitin: mode of action. 450 53

Two RNA polymerase activities were characterized in the cytoplasm of influenza Ao/NWS infected cells. Their relationship to the virion-associated RNA polymerase was studied.
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PMID:Relationship between the RNA polymerase activities from influenza virions and influenza virus-infected cells. 481 Oct 8

The addition of 5 mM dithiothreitol to a cell-free assay system for influenza ribonucleic acid (RNA) polymerase activity reverses the inhibitory activity otherwise possessed by three established antiviral compounds: selenocystine, 4-(2-propinyloxy)-beta-nitrostyrene, and acetylaranotin. Although 50% or greater enzyme inhibitory activity is repeatedly achieved for these compounds at a concentration of approximately 50 mug/ml (0.1 to 0.25 mM) in the absence of dithiothreitol, no inhibition is seen in its presence at inhibitor concentrations as high as 200 mug/ml. Against the deoxyribonucleic acid-directed RNA polymerases of Escherichia coli and chicken embryo cells, acetylaranotin and 4-(2-propinyloxy)-beta-nitrostyrene caused very little inhibition. Only selenocystine significantly inhibited these two enzymes in the absence of reducing agent, but to an extent substantially less than that obtained against the viral enzyme. These results appear to suggest that influenza RNA polymerase is uniquely sensitive to a variety of structurally diverse antiviral compounds as a consequence of their sulfhydryl reactivity-a fact which might aid in the search for and development of more potent chemotherapeutic agents.
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PMID:Sulfhydryl reactivity: mechanism of action of several antiviral compounds--selenocystine, 4-(2-propinyloxy)-beta-nitrostyrene, and acetylaranotin. 484 Apr 46

The products synthesized in vitro by an RNA-dependent RNA polymerase isolated from influenza virus-infected BHK21-F cells were analyzed by velocity sedimentation, annealing techniques, and acrylamide-agarose gel electrophoresis. Approximately 50% of the RNA synthesized in vitro remains associated with the 50 to 70S ribonucleoprotein complex containing polymerase activity; the remainder of the RNA polymerase product sediments heterogeneously with a peak at 13S. At least 90% of the in vitro product hybridizes with virion RNA. If polypeptides are labeled early in the growth cycle, both the P and NP polypeptides are detected in the ribonucleoprotein complex by acrylamide gel electrophoresis. The results suggest that the polypeptide composition and the products of the cell-associated RNA polymerase are similar to those of the RNA transcriptase associated with influenza virus particles.
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PMID:Analysis of the in vitro product of an RNA-dependent RNA polymerase isolated from influenza virus-infected cells. 485 84

The ribonucleic acid (RNA)-dependent RNA polymerase induced in the microsomal fraction of cells infected with influenza virus synthesized a mixture of single-and double-stranded RNA in vitro. The single-stranded RNA sedimented mainly in the 8S region on sucrose density gradients, with a smaller proportion of the RNA sedimenting at 18S. This sedimentation pattern corresponds closely to that of incomplete influenza virus RNA. The double-stranded RNA formed in vitro sedimented at 11S, but molecules which may be replicative intermediate, sedimenting at 14 to 20S, were also detected in the in vitro reaction product. Similar species of RNA were detected in vivo by pulse-labeling infected cells at the time of polymerase harvest, but the proportion of each RNA species was different, most of the RNA being single-stranded and sedimenting in the 18S region. An 11S double-stranded RNA was also synthesized in vivo. Pulse chase analysis of the double-stranded RNA synthesized in vitro showed that most is stable, and only a small proportion turns over during the reaction. A proportion of the RNA formed in vitro could be annealed to RNA formed in infected cells and to RNA extracted from purified virus.
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PMID:In vitro product of a ribonucleic acid polymerase induced by influenza virus. 548 Apr 8


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