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 reversible effect of dietary methionine deficiency was studied in young adult rats. The sensitivity of nuclear chromatin to micrococcal nuclease (EC3.1.4.7) digestion and the composition of the chromatin proteins were unaffected by the dietary regimens. The specific chromatin-bound RNA polymerase II activity decreased during methionine deficiency. Refeeding of methionine for 2 days restored the activity in the nuclease-released chromatin. RNA polymerase I plus III activity remained unchanged. Total RNA polymerase activity changed with the liver wet weight which was reduced during methionine deficiency and was not restored to control level after 2 days of methionine refeeding. RNA polymerase activity was altered by methionine deficiency. The recovery was independent of major modifications of the chromatin structure and protein composition.
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PMID:RNA polymerase activities and chromatin protein composition of rat liver during methionine deprivation and refeeding. 400 43

We have screened sera from patients with systemic lupus erythematosus for reactivity with RNA transcribed in vitro using HeLa whole cell extracts. Sera from 14 out of 114 patients precipitated an RNA transcribed by RNA polymerase III from a plasmid containing an Alu family sequence (i.e. the repetitive DNA sequence that is cut by the Alu restriction enzyme) located upstream from the human gamma G-globin gene. These Alu transcripts were not precipitated by anti-La, anti-Sm, anti-RNP or anti-Ro antibodies, suggesting that Alu RNA was precipitated by a previously undescribed lupus specificity. Analysis of [35S]methionine-labeled immunoprecipitates indicated that Alu RNA binds a protein of about 68 kDa. This protein may be Alu specific since three different Alu transcripts were precipitated by the anti-Alu sera whereas another RNA polymerase III transcript, adenovirus VA I RNA, was not precipitated by the same sera.
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PMID:Alu RNA-protein complexes formed in vitro react with a novel lupus autoantibody. 404 79

Poliovirus-infected HeLa cells were labeled with radioactive methionine or phenylalanine and subjected to a new purification procedure for the viral induced RNA polymerase activity. Detergent-solubilized polymerase activity was purified by precipitation with 2 M LiCl and sedimentation through sucrose gradients. Approximately 0.001% of the incorporated amino acid radio-activity sediments with the peak of polymerase activity. Gradient fractions comprising the polymerase activity peak were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and found to contain predominantly one virus-specific polypeptide. Polyacrylamide gel electrophoresis also reveals that this purified polypeptide migrates with a 58,000 molecular weight noncapsid polio-virus polypeptide.
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PMID:Isolation of a viral polypeptide associated with poliovirus RNA polymerase. 437 29

Previous data demonstrated that reovirus mRNA, synthesized in vitro with the particulate RNA transcriptase of reovirus cores, efficiently directs the synthesis of polypeptides in vitro. The present studies indicate that all of the three size classes of reovirus mRNA produced in vitro can form protein initiation complexes with rat liver [(36)S]Met-tRNA(F) and incubated 40S and 60S ribosomal subunits, which had been washed in 0.5 M KCl of mouse fibroblast L-929 cells. Mild prior treatment of the mRNA with HCHO was required to expose the initiator region. The initiation complex reacted quantitatively with puromycin to form a puromycin peptide, whose electrophoretic properties were identical to methionyl-puromycin formed in response to poly(A,G,U) or the initiator codon AUG. The complex was relatively stable and specific for [(35)S]Met-tRNA(F); rat liver [(35)S]Met-tRNA(M) was unreactive unless the supernatant factors EF T(1) and EF T(2) were also present. However, the addition of fusidic acid, at a concentration that did not affect complex formation with [(35)S]Met-tRNA(F), completely inhibited Met-tRNA(M) utilization. Exogenous ribosomal factors and GTP were not required unless the separated 40S and 60S subunits were further treated with 1 M KCl. The data suggest that reovirus mRNA contains AUG initiator codons that form a complex with Met-tRNA(F) at a puromycin-reactive site on ribosomes.
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PMID:Formation of a mammalian initiation complex with reovirus messenger RNA, methionyl-tRNA F , and ribosomal subunits. 450 35

Purified human reovirus contains RNA methylase activity in addition to an RNA polymerase. Virions incubated under appropriate conditions in the presence of S-adenosyl-L-methionine synthesize mRNA that is specifically methylated in the 5'-terminal guanosine. Alkaline digestion of the methylated RNA released a 5'-terminal dinucleotide, ppG'pCp, indicating that the guanosine contains 2'-O-methylribose. The possible roles of methylation in viral and cellular mRNA function is discussed.
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PMID:Methylated messenger RNA synthesis in vitro by purified reovirus. 452 44

The ribonucleic acid (RNA) bacteriophage phiCb5, which specifically infects only one form of the dimorphic stalked bacterium Caulobacter crescentus, has been obtained in high yield. Since the phage is extremely salt-sensitive, a purification procedure was devised which avoided contact with solutions of high ionic strength. Phage phiCb5 was studied with respect to the physical and chemical properties of both the phage and its RNA. In an electron microscope, the phage particles appear as small polyhedra, 23 nm in diameter. The phage is similar to the Escherichia coli RNA phages in that it (i) sediments at an S(20, w) of 70.6S, (ii) is composed of a single molecule of single-stranded RNA and a protein coat, (iii) contains two structural proteins, and (iv) apparently contains the genetic capacity to code for a coat protein subunit, a maturation-like protein, and an RNA polymerase. Phage phiCb5 differs from the E. coli RNA phages in (i) host specificity, (ii) salt sensitivity, and (iii) the presence of histidine, but not methionine, in the coat protein.
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PMID:Properties of Caulobacter ribonucleic acid bacteriophage phi Cb5. 549 12

The ethionine-induced genic derepression mechanism is visualized as a secondary process that occurs after the S-adenosyl-L methionine pool concentrations are lowered to critical levels. Although DNA methylation has been shown to be correlated with genic activity, the times observed for inducement (3 days) of the alpha-fetoprotein gene and its reversibility (within 7 days) does not make it likely that alterations in the methylated status of DNA is involved. The specific mechanism is theorized to be as follows: the adenine moiety of S-adenosyl-L-methionine base-pairs with thymine of a specific structural area of the alpha-fetoprotein gene. The process is visualized as a frequent event during moments of structural relaxation of an otherwise hyperspiralized condition of the chromatin. This weak hydrogen bonding situation allows the methylation by protein methylases of a precursor chromatin protein that after methylation by the S-adenosyl-L-methionine which is base-paired to the specific DNA site, conformationally is set or locked into place and acts as a specific repressor for the alpha-fetoprotein gene. This subsequently disallows RNA polymerase activity of the region. During turnover of this chromatin protein the replacement of the methylated repressor is normally maintained. But if the S-adenosyl-L-methionine pool concentration is lowered to a level below that required for base-pairing by the adenine moiety, then the repressed conformational condition of the alpha-fetoprotein gene is altered allowing transcription. In this manner the correlation between low S-adenosyl-L-methionine and alpha-fetoprotein synthesis can be made.
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PMID:Theoretical mechanisms for synthesis of carcinogen-induced embryonic proteins: XII mutational and non-mutational mechanism as subsets of a more general mechanism. Part A--Ethionine. 608 64

Several adenovirus early genes act together to promote growth of the helper-dependent adeno-associated virus (AAV). Data from several laboratories have implicated adenovirus early regions 1a, 1b, 2a, and 4 in the helper effect, as well as the small RNA polymerase III transcript, virus-associated RNA I. Although a subset of these must participate directly in the AAV life cycle, some may play an indirect role by influencing expression of the others. This paper is concerned particularly with the roles of early regions 1a and 1b in the helper effect. We introduced DNA fragments representing the various early regions into AAV-infected or uninfected Vero cells, by the manual microinjection procedure. After labeling the cells with [35S]methionine, we visualized immunoprecipitates of AAV or adenovirus proteins on sodium dodecyl sulfate-polyacrylamide gels. When over 200 copies of each DNA fragment per cell were injected, early regions 2a and 4 were themselves sufficient to provide the helper effect. At 100 copies per cell, however, a third gene became essential, and this could be either early region 1a or 1b. The role of early region 1a is easily explained by its known ability to stimulate transcription of the other early genes. The function of early region 1b is less clear, but it does not simply mimic the action of early region 1a. Instead, there appear to be at least two distinct regulatory pathways which can lead to expression of AAV. To investigate the sequence of regulatory interactions, we microinjected purified adenovirus mRNAs, or combinations of mRNA and DNA, into AAV-infected cells. Our results suggest that adenovirus early products enhance viral gene expression by several mechanisms which can operate independently, but whose effects may be cumulative.
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PMID:Requirement for either early region 1a or early region 1b adenovirus gene products in the helper effect for adeno-associated virus. 608 52

Isolated nuclei incorporate few methyl groups into RNA when they are incubated with S-adenosyl[methyl-3H3]methionine and four ribotriphosphates. When the nuclei were supplemented with a soluble total cell protein extract, the incorporation of methyl groups into RNA was stimulated 3-6-fold. All classes of RNA were methylated. Methylation of the 2'-OH of ribose and the bases of ribosomal RNA occurred predominantly on endogenous ribosomal RNA precursors, with a minority (20%) occurring on the newly synthesized rRNA precursor. Methylation of the tRNA precursor occurred on both endogenous (40%) and newly synthesized (60%) molecules. The methylation of adenosine in hnRNA occurred predominantly on molecules transcribed in vitro and was sensitive to 1 microgram/mL alpha-amanitin. A final site of methylation was the 7 position of guanosine of the cap structure. About 10% of the RNA polymerase II transcripts were capped in vitro. Capping was blocked 90% by 1 microgram/mL alpha-amanitin and was independent of the presence of the cell protein extract.
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PMID:Methylation of ribonucleic acid in a cell-free system from mouse myeloma cells. 618 6

Ibaraki virus core particles were purified from infected BHK-21 cells. The core particles displayed RNA transcriptase activity while the virion did not. The RNA transcriptase activity was stimulated about 15-fold by addition of S-adenosyl-L-methionine. The reaction product was single-stranded RNA which could be hybridized with heat-denatured Ibaraki virus RNA. The hybrids possessed the same electrophoretic mobility as Ibaraki virus double-stranded RNA.
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PMID:Characterization of ribonucleic acid transcriptase in Ibaraki virus core particles. 618 66


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