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)

The effects of magnesium and manganese in the initiation and elongation steps of the RNA polymerase I reaction in RNA synthesis were studied. For RNA chain initiation manganese was found to be a better effector than magnesium. For RNA chain elongation either manganese or magnesium acted as an effector, but a high concentration of manganese was inhibitory.
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PMID:Differences in the effects of manganese and magnesium on initiation and elongation in the RNA polymerase I reaction. 56 65

Multiple forms of RNA polymerases (I, II and III) from murine leukemia L1210 cells are solubilized, purified and characterized. Heterogeneity of RNA polymerases I and III is revealed by chromatography on DEAE-Sephadex and Phosphocellulose (P-11). The properties of these forms such as peculiarities of transcription of native and denaturated DNA, metal ion dependence (Mg2+, Mn2+ and (NH4)2SO4) and alpha-amanitin sensitivity resemble those reported for other mammalian RNA polymerases. The level of RNA polymerase I of leukemia L1210 cells increase approximately ten-fold relative to its level in some organs of healthy mice.
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PMID:[RNA-polymerase of murine leukemia L1210 cells]. 62 42

Escherichia coli RNA polymerase was assayed with 4 mM Mg2+ and 1 mM Mn2+ using native DNA, heat-denatured DNA, histone-nucleate and isolated rat liver nuclei as the template source. With purified DNA and either or both divalent metal ions, 0.1--5 mM amine stimulated enzyme activity. Spermidine resulted in the greatest stimulation (1.7-fold at 5 mM); whereas, spermine or methylglyoxal bis(guanylhydrazone) first stimulated, then above 3 mM inhibited, the reaction. The addition of unfractionated histone to purified DNA inhibited the reaction by 90%. The subsequent addition of amines resulted in a slight stimulation in incorporation (1.5-fold) in the range of 1--3 mM amine. Alternatively, when enzyme was combined with DNA before histone, only a 20% inhibition was observed and this could be completely prevented by 3 mM spermidine. The addition of amines to isolated nuclei resulted in marked alterations in ultrastructure and Mg2+ content; however, relatively small effects on RNA polymerase activity were observed. With the E. coli enzyme, 0.1--1.0 mM amine stimulated RNA synthesis (1.5-fold) whereas, none of the amines stimulated endogeneous activity in the absence or presence of 300 mM (NH4)2SO4.
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PMID:Effects of polyamines and methylglyoxal bis(guanylhydrazone) on Escherichia coli ribonucleic acid polymerase and the template activity of hepatic cell nuclei in vitro. 62 46

A cyclic AMP-dependent nuclear protein kinase was found to be closely associated with rat liver nucleolar RNA polymerase I throughout most of its purification. This protein kinase was purified to near homogeneity. It exhibits a number of unusual catalytic properties, including the inability to utilize Mn2+ when RNA polymerase is the substrate and the ability to phosphorylate both acidic and basic substrates. Phosphorylation of RNA polymerase I by this protein kinase results in the formation of phosphoester bonds characteristic of phosphoserine and phosphothreonine. Radioautography of polyacrylamide-gel electrophoretograms of the phosphorylated RNA polymerase I revealed that the 32P was located primarily on enzyme subunits SA1, SA3, SA5, and SA6 [nomenclature of Kedinger, Gissinger & Chambon (1974) Eur. J. Biochem, 44, 421-436].
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PMID:Purification and properties of a nuclear protein kinase associated with ribonucleic acid polymerase I. 62 59

Dimethylnitrosamine (DMNA) strongly inhibited RNA synthesis in mouse liver under conditions when the nucleotide pattern, rate of nucleotide synthesis and phosphorylation ratio were unaffected. (An unidentified, probably non-nucleotide, component in the acid-soluble liver fraction was selectively reduced.) The inhibition of RNA synthesis was associated with a decrease in the RNA polymerase activity of isolated liver nuclei, well established already 45 min after DMNA administration. The reduced activity included both Mg2+- and Mn2+/(NH4)2SO4-stimulated polymerase functions. The inhibition in vivo involved the whole complement of RNA, including poly (A)-containing RNA and isolated poly(A) sequences. The transfer of labelled RNA from the nucleus to the cytoplasm was not impaired. There was no detachment of poly(A)-containing RNA from the microsomes, and the proportion of tightly membrane-bound microsomal RNA and poly(A) sequences was not reduced as determined by use of a flotation technique. No breakage or shortening of the poly(A) chains was indicated by sedimentation analysis.
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PMID:RNA metabolism and poly(A) distribution in mouse liver following administration of dimethylnitrosamine. 66 22

RNA polymerase activity was measured in isolated cardiac nuclei subjected to hydrostatic pressure. After 20 min of pressure, Mn2+ stimulated RNA polymerase II activity was increased. The response to pressure was inhibited by low concentrations of alpha-amanitin (1.1 microgram.cm-3) an inhibitor of polymerase II activity. The data show that pressure applied to isolated nuclei stimulates RNA polymerase II activity, forming mRNA, and suggests that direct application of pressure to cardiac nuclei may be the stimulus which triggers the augmented protein synthesis seen in pressure overload.
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PMID:Effect of hydrostatic pressure on isolated cardiac nuclei: Stimulation of RNA polymerase II activity. 67 25

RNA synthesis in yeast is rapidly inhibited by 8-hydroxyquinoline and the phenazine antibiotic lomofungin (5-formyl-1-methoxycarbonyl-4,6,8-trihydroxyphenazine). It is shown that lomofungin, like 8-hydroxyquinoline, is a chelating agent for bivalent cations. The mechanism of inhibition of RNA synthesis by lomofungin and 8-hydroxyquinoline was investigated in experiments with isolated Escherichia coli RNA polymerase. The results show that both inhibitors are capable of inhibiting polymerase activity solely by chelating the dissociable cations Mn2+ and Mg2+. Evidence is presented which shows that inhibition may occur in the absence of any direct contact between the RNA polymerase or DNA template and the inhibitor. The possibility that inhibition might also occur by chelation of the Zn2+, which is tightly bound to the polymerase, is discussed: it is concluded that lomofungin or 8-hydroxyquinoline is likely to inhibit the enzyme by removal of Mn2+ and Mg2+ before chelating the Zn2+. On the basis of inhibition by chelation of Mn2+ and Mg2+, explanations are proposed for why lomofungin and 8-hydroxyquinoline inhibit synthesis of ribosomal and polydisperse RNA more than that of 5S RNA and tRNA, and for why protein synthesis is not immediately inhibited in the intact yeast cell.
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PMID:The mechanism of inhibition of ribonucleic acid synthesis by 8-hydroxyquinoline and the antibiotic lomofungin. 81 Jan 37

Two forms of RNA polymerase [EC 2.7.7.6], RPase L1 and RPase L2, isolated from a highly synchronized vegetative culture of Bacillus subtilis Marburg strain are described. RPase L1 is the major component (identical and the vegetative RNA polymerase already reported) and RPase L2 is a minor, new component corresponding to 3--5% of the total activity. The enzymes differed in their requirements for divalent ions, though the differences depended on the template DNA employed. PRase L1 is able to transcribe phage M2 DNA in the presence of Mg2+ ions and both B. subtilis DNA and phage M2 DNA in the presence of Mn2+ ions. On the other hand, RPase L2 activity can be detected only in the presence of 3 mM Mn2+ ions with all the templates. It is of interest that the transcription of phage M2 DNA by both enzymes stringently requires KC1. It may be due to this ion dependence that RPase L2 has not been detected previously. RPase L2 consists of 1beta', 1beta gamma, 1sigma, and 2alpha subunits. The molecular weight of the beta gamma subunit (about 110,000) is close to the value reported for the beta subunit of RNA polymerase prepared from sporulating cells. However, RPase L2 as a whole molecule is different from the RNA polymerase of sporulating cells or spores in the following two respects: RPase L2 contains sigma subunit as a component essential for selective transcription, and it is resistant to 1 mug of rifampicin per ml. Elimination of the sigma subunit from RPase L2 greatly stimulates RNA synthesis by the enzyme. Conversely, the addition of sigma subunit to the core-enzyme is inhibitory.
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PMID:RNA polymerase in vegetative cells of Bacillus subtilis. I. Purification and properties of RNA polymerase L1 and L2. 82 46

The effect of the dye aurintricarboxylic acid (ATA) on RNA polymerases [EC 2.7.7.6] solubilized from rat liver was studied. Complete inhibition of RNA synthesis in vitro was observed when 3-5 microng/ml of ATA was added to the reaction mixture at time 0, while 40-70 microng/ml of a rifampicin derivative, AF/013, was required to produce the same extent of inhibition. RNA formation, however, continued at a rate of one-half that of the control when ATA was given after the onset of RNA synthesis in a dose capable of completely blocking RNA formation if administered at time 0. ATA was found to interact with RNA polymerizing enzyme itself and competed specifically with the binding of RNA polymerase to template DNA. Preincubation of the enzyme with DNA at 37 degrees before adding dye made the DNA-enzyme complex partly resistant to the drug. RNA-synthesizing activity resistant to ATA increased when nucleoside triphosphates, especially GTP, were added to the preincubation mixture in the presence of Mn2+. However, ATA only slightly affected RNA synthesis in nuclei isolated from rat liver.
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PMID:The effect of aurintricarboxylic acid on RNA polymerase from rat liver. 84 32

RNA biosynthesis catalyzed with DNA-dependent RNA polymerase was demonstrated in the reconstructed system containing isolated lymphocyte nuclei, Mg2+ or Mn2+ salts, ammonium sulphate, in the presence of four nucleosidetriphosphates. Both the Mg2+ and Mn2+-dependent forms of this enzyme were revealed in the nuclei of normal lymphocytes and those of patients suffering from melanoma, carcinoma of the lung and sarcoma. The activities of both forms of RNA-polymerase were greater in the nuclei of the lymphocytes from sick individuals than in the normal analogues. DNA-dependent RNA-polymerase sensitivity to dexamethasone and PHA of the nuclei of lymphocytes obtained from patients with carcinoma of the lung, melanoma, and sarcoma was decreased in comparison with the normal.
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PMID:[Sensitivity of the lymphocyte RNA-synthesizing system of patients with different malignant neoplasms to phytohemagglutinin and dexamethasone]. 85 72


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