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)

A computer analysis of the operons containing Escherichia coli RNA polymerase subunits was carried out to obtain information about the regulation in the synthesis of these subunits, identifying intercistronic promoter and terminator sequences and searching for ribosome-binding sites and possible secondary structures of the corresponding mRNAs. This investigation showed an extensive secondary structure of beta-mRNA, which provides a molecular basis for the mechanism of the phenomenologically known post-transcriptional regulation in the synthesis of beta subunit. Since a similar secondary structure was also recognized in the mRNA corresponding to the upstream part of alpha subunit gene, it is proposed that the synthesis of alpha subunit is autogenously regulated by RNA polymerase itself, probably at the translational level, in the same way as in the synthesis of beta subunit. This regulation not only guarantees the suppression of overproduction of RNA polymerase subunits but also throws light on the problem of how the syntheses of RNA polymerase and ribosome respond similarly to the shift of nutrients and temperature, but differently to the starvation for amino acids.
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PMID:Regulation in the synthesis of Escherichia coli RNA polymerase proposed from sequence analysis. 306 79

In the ciliate Tetrahymena pyriformis phosphorylation of RNA polymerase I [EC 2.7.7.6] and of polymerase-associated polypeptides was investigated in growing and growth-arrested cultures which differ widely in their rates of rRNA synthesis. Several putative subunits of RNA polymerase I (of 180, 21.5, and 19.5 kDa) and a polymerase-associated polypeptide of 27 kDa were found to be phosphorylated, independent of the growth conditions. However, an additional enzyme-associated polypeptide of 26 kDa was intensively labeled with 32P only after arrestment of growth by starvation. The molar quantities of both phosphorylated, enzyme-associated polypeptides thereby did not differ in growing and growth-arrested cultures, and the specific 32P-labeling of cellular ATP remained nearly unchanged under the different culture conditions. These findings indicate a selective, reversible phosphorylation of the RNA polymerase I-associated 26 kDa polypeptide correlated with conditions of repressed rRNA synthesis induced by the starvation procedure. In vitro phosphorylation in macronuclei isolated from growing and growth-arrested cultures using [gamma-32P]ATP revealed essentially the same pattern of labeling of the enzyme-associated polypeptides of 27 and 26 kDa as it was found in vivo.
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PMID:Phosphorylation of RNA polymerase I-associated polypeptides of Tetrahymena pyriformis. 310 44

The 5' region of the rRNA operon, rrnA, of M. capricolum was cloned. Sequence analysis revealed two tRNA genes, tRNA(leu) and tRNA(lys), upstream to the promoter of the rRNA operon. The in vivo transcription start sites of the rRNA operon and of the tRNA genes were mapped. The same promoters used by M. capricolum RNA polymerase are also recognized by E. coli RNA polymerase both in vivo and in vitro. We find that high levels of ppGpp in E. coli, resulting from amino acid starvation or from spoT mutation, activate rather than repress the transcription of the mycoplasma rrnA operon.
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PMID:Promoters of Mycoplasma capricolum ribosomal RNA operons: identical activities but different regulation in homologous and heterologous cells. 334 May 43

The growth-rate regulation of transcription of the Escherichia coli tyrT gene depends on sequences in at least two distinct regions of the promoter, the upstream element required for optimal activity and the discriminator adjacent to the transcription start-point. Since mutations in the discriminator also alter the response of the promoter to amino acid starvation, we conclude that growth rate and amino acid control mechanisms share a common target molecule, probably RNA polymerase.
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PMID:Alteration of the growth-rate-dependent regulation of Escherichia coli tyrT expression by promoter mutations. 353 7

In prokaryotic organisms, the control of gene expression is mediated by regulatory proteins that activate or repress transcription. However, the molecular mechanisms of positive and negative control are different. In terms of negative control, repressor proteins bind to sites located within the promoter region and as a consequence sterically interfere with functional binding by RNA polymerase. Here, I examine the properties of a regulatory sequence that specifies catabolite (glucose) repression in the yeast Saccharomyces cerevisiae. Specifically, a DNA segment containing this regulatory site was fused upstream of the intact his3 promoter region and structural gene at several locations. Normally, his3 expression in these derivatives occurs at a basal level which can be induced by conditions of amino-acid starvation. However, in glucose medium, the catabolite regulatory sequence overrides the normal his3 promoter elements and reduces transcription both in normal and starvation conditions. The implication from these results is that in contrast to catabolite repression in Escherichia coli, which is mediated by catabolite-activating protein (CAP), catabolite repression in yeast occurs by a negative control mechanism involving a putative repressor protein. The observation that this regulatory site exerts its repressing effects even when located upstream of an intact promoter region suggests that repression in yeast is not mediated by steric interference between regulatory proteins and the transcriptional apparatus.
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PMID:Negative control at a distance mediates catabolite repression in yeast. 390 16

The yeast GCN4 gene product is necessary for the transcriptional induction of many amino acid biosynthetic genes in response to conditions of amino acid starvation. We synthesized radioactively pure GCN4 protein by in vitro translation of mRNA produced by in vitro transcription with SP6 RNA polymerase. GCN4 protein binds specifically to the 20 bp region of the HIS3 gene that is critical for transcriptional regulation in vivo and contains the TGACTC sequence common to coregulated genes. A synthetic GCN4 mutant protein lacking the 40 C-terminal amino acids fails to bind DNA; this correlates with a gcn4 mutant gene that is nonfunctional in vivo. Finally, GCN4 protein binds to the promoter regions of coordinately regulated genes, but not to analogous regions of other genes. We suggest that GCN4 protein is a specific transcription factor, and we describe a molecular model for the general control of amino acid biosynthetic genes.
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PMID:GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. 390 51

The growth of MCF-7 cells was arrested by 24 h of isoleucine deprivation. Following replenishment of the medium, the incorporation of uridine and thymidine into trichloroacetic acid-precipitable material began to increase slowly and gradually rose to the level of cycling cells. The addition of 5 X 10(-9) M estradiol to growth-arrested cells dramatically shortened the time of onset of macromolecular synthesis and increased the overall amount of precursor incorporation 2- to 4-fold over the level obtained by arrested control cells. The increase in uridine incorporation preceded the increase in thymidine incorporation by 6 h. Inhibition of protein synthesis with cycloheximide blocked the recovery of macromolecular synthesis in both control and estrogen-treated cells. Actinomycin D was ineffective in blocking the estrogen-stimulated recovery of macromolecular synthesis at concentrations known to inhibit pre-rRNA synthesis (10(-8) M). At higher concentrations, uridine and thymidine incorporation were inhibited in a dose-dependent manner. Inhibition of RNA polymerase II activity with alpha-amanitin similarly blocked both the recovery of the cells from isoleucine starvation and the potentiation of this by estradiol. Dihydrofolate reductase and thymidine kinase activities are both stimulated by estradiol in MCF-7 cells. In cycling cells, estrogen stimulates a 2-fold increase in their messenger RNAs (mRNAs) within 24 h. The level of dihydrofolate reductase mRNA is unaffected by isoleucine starvation, and estrogen caused no change in dihydrofolate reductase mRNA levels over a 24-h period following reversal of growth arrest. Similar results were observed for the 600-nucleotide pS2 mRNA that has been identified as an estrogen-induced RNA in MCF-7 cells. In contrast, thymidine kinase mRNA was found to be increased by estrogen at 24 h, but not at 12 h, following reversal of growth arrest. This increase correlates with increases in thymidine, but not uridine incorporation. These data indicate that the estrogen-stimulated increase in thymidine incorporation following release from growth arrest is dependent on new RNA synthesis. However, the hormone did not increase the levels of three estrogen-regulated mRNAs coordinately with the increases observed in uridine incorporation.
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PMID:Relationship between the expression of estrogen-regulated genes and estrogen-stimulated proliferation of MCF-7 mammary tumor cells. 398 99

In glutaraldehyde-prefixed exponential-phase cells of Streptococcus faecalis the nucleoid is "frozen" in a dispersed configuration. Exposure of exponential-phase cells to threonine starvation or to antibiotics inhibiting protein synthesis resulted in progressive condensation of nucleoid fibrils producing an expanding central nucleoid zone or pool. The condensation of the nucleoid was observed to occur at a rate directly proportional to the rate of inhibition of protein synthesis. However, the extent of nucleoid condensation depended on continuing deoxyribonucleic acid synthesis. Significantly less nucleoid condensation occurred when cells were inhibited in deoxyribonucleic acid and protein synthesis than when cells were inhibited in protein synthesis alone. These results suggest a model in which, during nucleoid replication, the chromosome fibrils are normally maintained in a dispersed state by the active agents of transcription-translation, such as ribonucleic acid polymerase molecules and ribosomes.
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PMID:Morphokinetic reaction of Streptococcus faecalis (ATCC 9790) cells to the specific inhibition of macromolecular synthesis: nucleoid condensation on the inhibition of protein synthesis. 411 Sep 25

Amino acid starvation of "stringent RNA control" (RC(str)) strains of Escherichia coli (E. coli) results in the cessation of net protein and net RNA synthesis, whereas "relaxed RNA control" (RC(rel)) strains continue net RNA synthesis under the same conditions of amino acid starvation. This report tests further the hypothesis that net RNA synthesis is markedly reduced during amino acid starvation of RC(str) strains as a result of reduction in the supply of substrates of the RNA polymerase. Bacterial ribonucleoside triphosphate pool levels were measured before and after the arrest of protein synthesis in RC(str) and RC(rel) strains. Protein synthesis was inhibited either by addition of trimethoprim to the medium or by the use of a mutant having a temperature-sensitive valyl-tRNA synthetase. The ribonucleoside triphosphate pool levels do not decline significantly during inhibition of protein synthesis in RC(str) strains under either condition, and there is no apparent correlation between the measured pool levels and the residual rate of net RNA synthesis in RC(str) and RC(rel) strains. Thus, these data argue against the hypothesis that the regulation of RNA synthesis is mediated by the availability of substrates of the RNA polymerase.
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PMID:Nucleoside triphosphate pools and the regulation of RNA synthesis in E. coli. 489 29

1. Experiments with rifampicin and stringent strains of Escherichia coli (pro(-)purB(-)rel(+)) indicate that purine deficiency does not decrease and may considerably increase the potential for RNA synthesis by RNA polymerase molecules that are bound to DNA and have already commenced transcription. 2. DNA-RNA hybridization experiments indicate that purine starvation increases the distribution of bound RNA polymerase molecules between the cistrons for mRNA and those for stable RNA. 3. Synthesis of beta-galactosidase mRNA is more dependent on the ability to synthesize guanine nucleotides than on the ability to synthesize adenine nucleotides. 4. Amino acid starvation tends to decrease the potential for RNA synthesis by RNA polymerase molecules bound to DNA. 5. Since this effect differs from that due to purine starvation, amino acid control of RNA synthesis does not appear to operate solely by causing a deficiency of purine nucleotides. 6. The results are discussed in terms of the ability to initiate RNA chains and to extend them under different circumstances.
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PMID:Synthesis of ribonucleic acid in purine-deficient Escherichia coli and a comparison with the effects of amino acid starvation. 492 43


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