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 mRNA transcripts of Rhodospirillum rubrum gene puh, coding for the H subunit of the photoreaction center, and of genes flanking puh were analyzed by blot hybridization. Open reading frame G115, upstream of structural gene puh, is transcribed as a 2.25-kilobase mRNA. Gene puh itself is transcribed as two mRNAs of 1118 and 1032 nucleotides. Mung bean nuclease protection analysis shows that the puh transcripts have different 5' termini within open reading frame G115 and a unique rho-independent termination signal within open reading frame I2372. The lifetimes of the puh messages, as determined by an oxygen blockade of transcription, were 10 and 12 min for the large and small puh mRNAs, respectively. An expression vector carrying a chloramphenicol acetyltransferase gene was used to select promoters in DNA stretches upstream of the startpoints of each of these transcripts. Chloramphenicol resistance was expressed in Escherichia coli, using as a promoter a 179-nucleotide stretch upstream of the small mRNA startpoint but not from a 124-nucleotide stretch upstream of the large mRNA startpoint. The promoter for the small mRNA, designated Ppuh2, is thought to encompass in its -10 and -35 regions a sigma 70-like RNA polymerase recognition sequence. The region upstream of the large message startpoint contains a sequence similar in its -12 and -24 regions to promoter sequences recognized by the sigma 60 RNA polymerase holoenzyme. This is designated as promoter Ppuh1.Ppuh1 is proposed to be strictly regulated by light intensity and by oxygen tension while Ppuh2 would be less sensitive to these parameters.
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PMID:Mapping of the puh messenger RNAs from Rhodospirillum rubrum. Evidence for tandem promoters. 249 83

The amatoxins, highly toxic components of Amanita mushrooms, strongly inhibit the DNA-dependent RNA polymerase II (or B) in eukaryotic cell nuclei. For optimal binding to the enzyme a gamma-hydroxyisoleucine side chain in the 3-position is important as in gamma-amanitin (compound 1), where the OH-group is bound in the [S]-configuration. Amanullin, a non-toxic component, having an oxygen-free isoleucine side chain no. 3, exhibits an inhibitory effect on RNA polymerase II about two orders of magnitude smaller than that of gamma-amanitin. An equal, relatively weak, inhibitory effect has previously been found with the synthetically obtained Ile3-analog 7. In the present paper the synthesis of an analog (2) bearing a gamma-hydroxyl group in the isoleucine side chain is described. The compound was found to have about the same inhibitory effect on RNA polymerase II from Drosophila embryos as amanullin and the Ile3-analog 7. Structure analysis by X-ray diffraction revealed that the hydroxyl group at the -carbon atom of side chain-3 has the [R]-configuration, the new analog thus being -deoxo[( )-hydroxy-[Ile3]-amaninamide. It follows that the [S]-configuration of this chiral center is a prerequisite to maximal toxicity. Crystallographic data demonstrating great similarity between the peptide backbones of the new analog and those of natural amatoxins are given.
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PMID:Structure-toxicity relationships in the amatoxin series. Synthesis of S-deoxy[gamma(R)-hydroxy-Ile3]-amaninamide, its crystal and molecular structure and inhibitory efficiency. 259 60

Hybrid 5' regulatory regions were constructed in which the upstream activator sequence (UAS) and promoter of various nif genes were exchanged with the upstream regulatory sequence (URS) of the fdhF gene from Escherichia coli. They were analysed for their regulatory response under different growth conditions with the aid of fdhF'-'lacZ or nif'-'lacZ fusions. Placement of the UAS from the Bradyrhizobium japonicum nifH gene in front of the spacer (DNA region between URS and promoter) plus promoter from fdhF renders fdhF expression activatable by the Klebsiella pneumoniae NIFA protein, both under aerobic and anaerobic conditions. This excludes the possibility that the spacer of the fdhF5' flanking region contains a site recognized by a putative oxygen- or nitrate-responsive repressor. There was also considerable activation by NIFA of fdhF expression in a construct lacking the nifH UAS but containing the fdhF spacer plus promoter. Further experimental evidence suggests that this reflects a direct interaction between NIFA and RNA polymerase at the ntrA-dependent promoter. A second set of hybrid constructs in which the URS from fdhF (E. coli) was placed in front of the nifD spacer plus promoter from B. japonicum or in front of the K. pneumoniae nifH, nifU, nifB spacers and promoters, delivered inactive constructs in the case of the nifD, nifU and nifB genes. However, a nifH'-'lacZ fusion preceded by its own spacer and promoter plus the foreign fdhF URS displayed all the regulatory characteristics of fdhF expression, i.e. anaerobic induction with formate and repression by oxygen and nitrate. Although it is not known why only one out of the four nif promoters could be activated by the fdhF URS, this result nevertheless demonstrates that the various regulatory stimuli affecting expression of fdhF in E. coli have their target at the upstream regulatory sequence.
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PMID:Construction of chimaeric promoter regions by exchange of the upstream regulatory sequences from fdhF and nif genes. 266 22

The Rhizobium meliloti nifA product (NifA) shares extensive homology in its central region and at its C-terminal end with Rhizobium leguminosarum DctD and with NtrC from several species. All three proteins are transcriptional activators of NtrA (RpoN)-RNA polymerase-dependent promoters. Several large deletions of R. meliloti NifA were constructed to investigate the role of the conserved and divergent domains of NifA in transcriptional activity and posttranscriptional regulation by oxygen. The ability of NifA expressed from the Escherichia coli lacZ promoter to activate the R. meliloti nifH promoter in E. coli and R. meliloti was tested under a range of defined atmospheric oxygen partial pressures. Deletion of the divergent N-terminal domain of NifA had little effect on NifA activity and no effect on oxygen sensitivity. Deletion of the conserved C-terminal helix-turn-helix motif of NifA did not eliminate NifA-dependent activation of the nifH promoter, although it did decrease NifA activity about twofold in E. coli and 10-fold in R. meliloti. A NifA carrying both the N-terminal and C-terminal deletions and consisting of only the central highly conserved domain and 50 divergent amino acids retained the ability to activate transcription from the nifH promoter. The transcriptional activity of the conserved central domain is consistent with the prediction that the core domain is the part of NifA which interacts with the transcriptional machinery to stimulate transcription.
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PMID:The central domain of Rhizobium meliloti NifA is sufficient to activate transcription from the R. meliloti nifH promoter. 272 51

Mono- and bisthiopyrophosphate can inhibit the replication of influenza virus A/X49 in Madin-Darby canine kidney (MDCK) cells at concentrations at which no cytotoxic effect is observed after 3 days. The thiopyrophosphate analogues inhibit the RNA transcriptase activity of this virus possibly by chelating with an essential metal ion in the transcriptase complex. [31P]NMR spectroscopy indicates that bisthiopyrophosphate coordinates to zinc through sulphur and magnesium through oxygen which may influence the inhibitory properties of this compound with metal-containing enzymes.
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PMID:Thio-analogues of inorganic pyrophosphate inhibit the replication of influenza virus A in vitro. 299 Mar 33

In an attempt to identify features of an oxygen-regulated promoter, we have determined the location of transcription initiation for the puf operon. The position for the oxygen-regulated promoter was demonstrated by several independent means to be located 699 base pairs (bp) upstream from the pufB structural gene. DNA sequence analysis of the promoter region demonstrates the presence of a 26-base pair region of dyad symmetry followed by a sequence containing homology to promoters which use the RNA polymerase sigma 60 subunit (ntrA) for recognition of DNA. In addition to the oxygen-regulated promoter, a region responsible for low-level constitutive expression of the puf operon was shown to initiate transcription 511 bp upstream from the pufB gene. In contrast to the oxygen-regulated promoter, this second promoter contains no obvious secondary structure nor sequence homology to ntrA-dependent promoters. DNA sequence analysis demonstrates the existence of an additional open reading frame (designated as pufQ) that is located between the promoters and the pufB structural gene. A translational fusion of pufQ to lacZ was used to demonstrate that pufQ is efficiently translated and regulated in a manner analogous to a translational fusion of pufM to lacZ. Finally, we also demonstrate that puf operon transcription initiation and regulation does not involve any puf-encoded gene products.
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PMID:Analysis of the Rhodobacter capsulatus puf operon. Location of the oxygen-regulated promoter region and the identification of an additional puf-encoded gene. 312 91

Metallothioneins that bind copper and zinc have an Mr of 6500 daltons, consist of a single polypeptide chain of 61 amino acids, 25-30 percent of whose residues are cysteine, have a metal-binding capacity of between 5 and 7 g atoms/mol, and contain no disulfide bonds or aromatic amino acids. Zincthionein has been postulated to participate in the transport and storage of zinc, which is involved in more than 235 metalloenzymes, including thymidine kinase, RNA polymerase, and ribonuclease, which in turn play crucial roles in the replication and transcription of DNA during cell division. In addition, trace elements including zinc modulate immune response and function. Conversely, zinc deficiency state causes, for example, thymic atrophy and lymphopenia and modifies antibody-mediated responses to both T-cell-dependent and T-cell-independent antigens. The concentrations of copper, zinc, and metallothionein and the copper/zinc ratio are modified in a number of malignancies. For example, the levels of metallothionein in normal and in malignant human livers are 471 and 75 micrograms/g, respectively. In addition, the copper/zinc ratio is significantly increased in human pancreatic cancer from 1.40 to 2.70. Furthermore, studies involving 64Cu in tumor-bearing mice showed that the distribution of 64Cu was altered and that all tumors contained a relatively high level of 64Cu. Moreover, the activity of superoxide dismutase to remove free oxygen radicals is lower in malignant tissues. Finally, the results of clinical studies suggest that the monitoring of the serum copper/zinc ratio may be a valuable tool, not only in determining the extent of malignancies, but also in predicting the efficacy of treatments.
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PMID:The status of zinc, copper, and metallothionein in cancer patients. 328 43

We have developed general methods for joining together, via cleavable disulfide bonds, either two unprotected polynucleotides or a polynucleotide and a peptide or protein. To join two oligonucleotides, each is first converted to an adduct in which cystamine is joined to the 5'-terminal phosphate of the oligonucleotide by a phosphoramidate bond. The adducts are mixed and reduced with dithiothreitol. The dithiothreitol is then removed by dialysis. Oxidation by atmospheric oxygen occurs to yield the required dimer. To join an oligonucleotide to a cysteine-containing peptide or protein, the 5'-cystamine oligomer is first converted to a 2'-pyridyldisulfide adduct and then reacted with an excess of the peptide or protein. If the peptide does not contain a free cysteine residue, it is first treated with iminothiolane to introduce one or more sulfhydryl groups. We have used these procedures to join a 16 mer deoxynucleotide probe and MDV-1 RNA, a substrate of Q beta RNA polymerase. This adduct hybridizes with a complementary target DNA. We have also joined a 16mer probe to peroxidase and MDV-1 RNA to human IgG. The probe-peroxidase adduct maintains enzymatic activity and the MDV-1 RNA-IgG adduct binds to a complementary anti-IgG.
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PMID:Ligation of oligonucleotides to nucleic acids or proteins via disulfide bonds. 337 70

The single large heat-responsive puff (hs puff) in polytene foot pad cells of fly pupae (Sarcophaga bullata) is shown to be inducible by oxygen deprivation but not, as in other systems, by reoxygenation following an hypoxic treatment. The ambient oxygen concentration must drop below 2% for the hs puff to be maximally induced but the puff is fully inducible and transcriptionally active even in the complete absence of oxygen. Lack of oxygen is also compatible with continued transport of puff materials (formation and dissipation of puff droplets at the hs locus). Hypoxia-induced hs puffs persist indefinitely (greater than 2 days) at maximal or intermediate size and only regress completely after oxygen is resupplied. The induction of the hs puff during hypoxia is highly specific and does not seem to involve activation of any other chromosomal loci, yet the reaction is not confined to the giant foot pad cells or to specific developmental stages. Azide poisoning of cultured foot pads simulates the in vivo effects of hypoxia. The induction of the hs puff by azide, heat, or other means is inhibited by sulfhydryl reagents (iodoacetamide, arsenite) and fluoride, but not by an inhibitor of substrate-linked phosphorylation (arsenate). Instead, arsenate, like other uncouplers (2,4-dinitrophenol) is an inducer of the hs locus. The hs puff can be fully induced by hypoxia at any temperature between 2 degrees and 45 degrees C. The rate of puff expansion is strictly temperature dependent and the temperature characteristics of this process are remarkably similar to those of a promoter RNA polymerase association.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Induction of a heat shock puff by hypoxia in polytene foot pad chromosomes of Sarcophaga bullata. 369 49

Oxygen enhanced the bactericidal activity of rifamycin SV to Escherichia coli K12. Anaerobically grown cells, which had a low level of superoxide dismutase, were more susceptible to the bactericidal activity than aerobically grown cells, which contained a high level of superoxide dismutase. Oxygen also enhanced the inhibition of RNA polymerase activity of rifamycin SV, when Mn2+ was used as a cofactor. Rifamycin S was reduced to rifamycin SV by NADPH catalyzed by cell-free extracts of Escherichia coli K12. These results indicate that the inhibition of bacterial growth by rifamycin SV is due to the production of active species of oxygen resulting from the oxidation-reduction cycle of rifamycin SV in the cells. The aerobic oxidation of rifamycin SV to rifamycin S was induced by metal ions, such as Mn2+, Cu2+, and Co2+. The most effective metal ion was Mn2+. In the presence of Mn2+, accompanying the consumption of 1 mol of oxygen and the oxidation of 1 mol of rifamycin SV, 1 mol of hydrogen peroxide and 1 mol of rifamycin S were formed. Superoxide was generated during the autoxidation of rifamycin SV. Superoxide dismutase inhibited the formation of rifamycin S, but scavengers for hydrogen peroxide and the hydroxyl radical did not affect the oxidation. A mechanism of Mn2+-catalyzed oxidation of rifamycin SV is proposed and its relation to bactericidal activity is discussed.
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PMID:Oxygen Enhancement of bactericidal activity of rifamycin SV on Escherichia coli and aerobic oxidation of rifamycin SV to rifamycin S catalyzed by manganous ions: the role of superoxide. 627 85


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