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 artificially stimulated decidual cell reaction has been used as a model to study changes occurring in the uterus at the time of implantation. Activities of RNA polymerases I, II and III were measured in uterine nuclei isolated from ovariectomized non-primed mice, hormonally primed mice, and hormonally primed mice following stimulation of the decidual cell reaction. Activities of all three RNA polymerases increased following hormonal priming of ovariectomized mice. In nuclei from stimulated uterine horns, activities of RNA polymerases I and III increased 9 h after stimulation of the decidual cell reaction and remained elevated through 21 h. RNA polymerase II activity did not change following stimulation of the decidual cell reaction. These changes in RNA polymerase activities occur at the time of increased histone modifications and may result from changes in the template capacity.
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PMID:Changes in RNA polymerase activity in isolated mouse uterine nuclei during the decidual cell reaction. 71 31

The in vitro transcription of chick liver chromatin before and after estrogen treatment was studied. Transcription was by endogenous as well as homologous exogenous RNA polymerase II and the products were analyzed for size and specific vitellogenin sequences. Quantitatively more RNA was synthesized from chromatin of 24 h estrogen-treated (E 24) chicks than from that of untreated chicks. In either case the size of transcribed RNA ranged from 5S to larger than 28S and most was between 5S and 18S. When a fraction enriched in estrogen receptor (E-Rec) complex was added to chromatin from untreated chicks, a dramatic shift of the RNA transcribed into heavier regions occurred. Analysis of RNA transcripts by hybridization to cDNAvit showed an equal number of sequences transcribed from E 24 chromatin and control; however, 13 times more specific sequences were transcribed in the presence of E-Rec complex. The results indicate the E-Rec complex exerts a regulatory function in the specific transcription of the vitellogenin gene.
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PMID:In vitro transcription of vitellogenin sequences on chick liver chromatin. 72 4

Embryos and larvae of the brine shrimp, Artemia salina, provide a useful biological system for biochemical studies of animal development. Dormant encysted embryos can be cultured readily in the laboratory to provide large quantities of free-swimming nauplius larvae. The rate of synthesis of all classes of RNA in swimming larvae declines markedly between 24 and 72 h after immersion of dormant embryos in sea water. Nuclei were isolated from 24-72 h larvae and RNA polymerase activity was measured under conditions in which the nuclei remained intact. Total RNA polymerase activity of isolated nuclei decreased in parallel with RNA synthesis in vivo. RNA polymerases were solubilized from nuclei and fractionated by chromatography on DEAE-cellulose. The levels of both RNA polymerases I and II also decreased in parallel with RNA synthesis in vivo. The specific activity of highly purified RNA polymerase II was determined by comparison of enzyme activity with the mass of RNA polymerase II subunits displayed on SDS gels. The specific activities of RNA polymerase II preparations from 24 and 72 h larvae were identical. The number of polymerase II molecules was estimated from the mass of the subunits. The number of molecules per nucleus declined from 20,000 at 24 h to 3500 at 72 h.
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PMID:DNA-dependent RNA polymerases from Artemia salina: decreasing polymerase activities and number of polymerase II molecules in developing larvae. 72 50

The hypothesis of functional hemizygosity has been examined for the alpha-amanitin resistant (AmaR, a codominant marker) locus in a series of Chinese hamster cell lines. AmaR mutants were obtained from different cell lines, e.g., CHO, DHW, M3- 1 and CHO-Kl, at similar frequencies. After fractionation of different RNA polymerase activities in the extracts by chromatographic procedures, the sensitivity of the mutant RNA polymerase II towards alpha-amanitin was determined. While all of the RNA polymerase II activity in mutant CHO and CHO-Kl lines became resistant to alpha-amanitin inhibition, only about 50% of the activity is highly resistant in AmaR mutants of CHW and M3- 1 cell lines. The remaining activity in the latter cell lines shows alpha-amanitin sensitivity similar to that seen with the wild-type enzyme. This behaviour is similar to that observed with a 1:1 mixture of resistant and sensitive enzymes from CHO cells. These results, therefore, strongly indicate that while only one functional copy of the gene affected by alpha-amanitin is present in CHO and CHO-Kl cells, two copies of this gene are functional in the CHW and M3-1 cell lines.
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PMID:Evidence for variation in the number of functional gene copies at the AmaR locus in Chinese hamster cell lines. 73 Jul 80

Castration results in a rapid decrease in the activity of RNA polymerase I (or A) of isolated nuclei of rat prostates. The decrease was mainly ascribed to the diminution in the number of in vivo initiated RNA chains. The "free form" activity of the enzyme, however, which was estimated by the use of exogenous template and actinomycin D, increased 24 h after castration, then dropped rapidly. The administration of testosterone to castrated rats caused an increase in the activities of both RNA polymerases I and II (or B), which started 2 h and reached the maximum 12 h after the administration. No initial rise in RNA polymerase II activity was observed during the first 2 h. The administration of cycloheximide to normal rats caused a very rapid decrease of the activity of template-bound RNA polymerase I of isolated prostatic nuclei (t1/2=1.7 h), while the "free form" activity of the enzyme did not appreciably change until 3 h. The androgen-stimulated increase in the "engaged form" of the RNA polymerase I of isolated nuclei was completely abolished by the administration of cyclohexmide 60 min before killing. Based on the results obtained, the role of protein(s) with a rapid turn-over which is/are androgen-dependent and presumably participating in the control of preibosomal RNA synthesis is discussed.
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PMID:In vivo effect of androgen and cycloheximide on the RNA synthesis in isolated nuclei of rat ventral prostates. 73 1

1. A nucleoplasmic fraction rich in endogenous RNA polymerase II activity was isolated from rat liver nuclei and conditions were determined under which elongation of RNA molecules initiated in vivo continued at maximal rates in vitro. 2. Elongation rates in vitro were calculated to be about 0.25 nucleotide/s and there were about 7 X 10(3) RNA molecules in the process of being elongated by form-II RNA polymerase per original nucleus. 3. Evidence was obtained suggesting that transcription-dependent release of RNA polymerase II molecules from the template occurred during the incubations in vitro. 4. The nascent RNA was tightly associated with protein and banded as ribonucleoprotein in caesium salt gradients. 5. RNA molecules labelled in vitro were up to 13000 nucleotides in length, but consisted of long unlabelled chains transcribed in vivo with only short labelled sequences added in vitro, and without significant polyadenylation. 6. Hybridization of transcripts in the presence of a vast excess of DNA demonstrated that both form-II RNA polymerase and another enzyme, resistant to low alpha-amanitin concentrations, were synthesizing RNA molecules complementary to both reiterated and unique DNA sequences in the genome.
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PMID:The use of rat liver nucleoplasm for the characterization of heterogeneous nuclear ribonucleic acid synthesis in vitro. 74 48

Intraperitoneal administration of cycloheximide (100 mg/kg) to rats produces a time-dependent rise in nuclear RNA polymerase II activity which is maximum at 30 min. This same concentration of cycloheximide also reduces RNA polymerase I activity to 64% of control within this time period. When 10 mg/kg of cycloheximide was administered, there was a 2-fold increase in both RNA polymerases II and III activities within 30 min as assayed in isolated nuclei. When these enzymes are solubilized from nuclei and resolved by DEAE-Sephadex, there is no significant change in the activity of RNA polymerase I or II when assayed on an exogenous template. It is suggested that the dual enhancement of nuclear RNA polymerase II and III activities is the result of a compensatory feedback relationship which exists between translation and transcription in vivo.
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PMID:Enhanced transcription by RNA polymerases II and III after inhibition of protein synthesis. 76 44

Three peaks of DNA-dependent RNA polymerase (RNA nucleotidyltransferase) activity are resolved by chromatography of a sonicated yeast cell extract on DEAE-Sephadex. The enzymes, which are named RNA polymerases I, II, and III in order of elution, show similar catalytic properties to the vertebrate class I, class II, and class III RNA polymerases, respectively. Yeast RNA polymerase III is readily distinguished from yeast polymerase I by its biphasic amnonium sulfate activation profile with native DNA templates, greater enzymatic activity with poly[d(I-C)] than with native salmon sperm DNA, and distinctive chromatographic elution positions from DEAE-cellulose (0.12 M ammonium sulfate) compared with DEAE-Sephadex (0.32 M ammonium sulfate). The three yeast RNA polymerases also show significant differences in alpha-amanitin inhibition. RNA polymerase II is the most sensitive (50% inhibition at 1.0 mug of alpha-amanitin per ml). Contrary to the results for vertebrate systems, yeast polymerase I can be completely inhibited by alpha-amanitin at high concentrations (50% inhibition at 600 mug/ml) while yeast RNA polymerase II BEGINS TO SHOW SIGNIFICANT INHIBITION ONLY AT CONCENTRATIONS EXCEEDING 1 MG/ML. Therefore, yeast RNA polymerases I and III show a pattern of alpha-amanitin sensitivity that is the reverse of that seen for the analogous vertebrate RNA polymerases.
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PMID:Transcription in yeast: alpha-amanitin sensitivity and other properties which distinguish between RNA polymerases I and III. 77 76

Hen oviduct RNA polymerase II and Escherichia coli RNA polymerase holoenzyme and core enzyme were used to study the initiation of RNA synthesis on chromatin. In either the presence or absence of estrogenic stimulation, changes in the level of oviduct chromatin initiation sites as measured in the presence of either homologous or heterologous polymerases followed a similar pattern. Comparison of the initiation sited utilized by these enzymes on chick oviduct chromatin indicated that these enzymes compete with each other for the same initiation regions. In contrast to chromatin, however, the majority of the initiation sites on DNA which are utilized by the oviduct RNA polymerase II are different from those utilized by E. coli holoenzyem. These results suggest that chromatin proteins are involved in the selection of initiation sites on chromatin for RNA polymerases. The in vitro transcripts of these RNA polymerases on stimulated chick oviduct chromatin were analyzed by hybridization to a cDNA probe transcribed from ovalbumin mRNA. The relative concentration of ovalbumin sequences transcribed by these three polymerases was 4:1.5:1 for oviduct RNA polymerase II, E. coli core enzyme, and holoenzyme respectively. Therefore, the efficiency of transcribing a specific gene appears to depend on the interaction between RNA polymerase and chromosomal elements in the initiation region.
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PMID:Effect of estrogen on gene expression in the chick oviduct. 77 31

Polar organic compounds, including DMSO, increase RNA synthesis on isolated chromatin by E. coli RNA polymerase and RNA polymerase II from calf thymus. Transcription is stimulated on chromatin from Friend-virus-infected erythroleukemia cells and from various other sources. Using procedures which inhibit specifically the formation of a stable initiation complex, it is shown that the stimulation does not result from an increase in initiation of both E. coli and the eukaryotic RNA polymerase. After separation of chromatin into template active and inactive fractions, DMSO increases RNA synthesis by a factor of about 1.5 using the template inactive fraction, while stimulation of transcription on the template active portion is lower (factor of 1.2). It is suggested that the effect on RNA synthesis is mediated by a weakening of the apolar interactions between histones in chromatin subunits, releasing transcription partially from the constraints imposed by histones.
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PMID:Stimulation of transcription on chromatin by polar organic compounds. 78 22


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