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 prokaryotic activator protein NTRC binds to enhancer-like elements and activates transcription in response to nitrogen limitation by catalysing open complex formation by sigma 54 RNA polymerase holoenzyme. Formation of open complexes requires the phosphorylated form of NTRC and the reaction is ATP dependent. We find that NTRC has an ATPase activity which is activated by phosphorylation and is strongly stimulated by the presence of DNA containing specific NTRC binding sites.
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PMID:The prokaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent. 153 52

Restriction fragments containing established curved regions, such as the pBR322 tn3 region, the phage lambda attP region and the SV40 T-antigen and terminus of replication regions, exhibit systematically retarded elution upon anion exchange based HPLC. Using this method, we were able to detect readily other SV40 curved regions, exhibiting also the polyacrylamide gel electrophoresis retardation anomaly, including several RNA polymerase initiation sites. Unlike gel retardation, HPLC retardation exhibited by curved DNA persists at 55 degrees C and is observed for fragments ranging from 150 bp up to 5 kb. The observed preferential attachment of DNA fragments containing curved DNA to the ionic groups of the column suggests a common dipole character of these regions due to the local accumulation of charges resulting apparently from the compression in the minor groove of curved DNA.
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PMID:Curved DNA fragments display retarded elution upon anion exchange HPLC. 165 80

The rat gastric H+/K(+)-ATPase beta subunit gene was cloned, and its nucleotide sequence was determined. The coding region is separated by 6 introns, whereas the related human Na+/K(+)-ATPase beta subunit gene was shown to have 5 introns (Lane, L.K., Shull, M.M., Whitmer, K.R., and Lingrel, J.B. (1989) Genomics 5, 445-453). The positions of introns 1, 2, and 5 of the two genes were the same. The similarities in intron/exon organizations and primary structures (30-40% identical residues) suggest that the beta subunit genes for H+/K(+)-ATPases were derived from a common ancestor. The upstream region of the rat H+/K(+)-ATPase beta subunit gene contains direct repeat sequences and palindromes, potential binding sites for RNA polymerase II and E4TF1, and CACCC box sequences. Gel retardation assay demonstrated that the stomach, but not other tissues (liver, brain, kidney, spleen, and lung), has a nuclear protein(s) capable of binding to the regions upstream of the potential RNA polymerase II binding sites (TATA box). The nuclear protein(s) are suggested to recognize three tandem GATAGC sequences and may be important for controlled transcription of the H+/K(+)-ATPase beta subunit gene in gastric parietal cells.
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PMID:The rat H+/K(+)-ATPase beta subunit gene and recognition of its control region by gastric DNA binding protein. 165 72

The autoantigen La, a known transcription termination factor of RNA polymerase III, was purified to homogeneity from mouse 3T3 cells and calf thymus by different isolation procedures. The La protein from calf thymus was separated into RNA binding and nonbinding subclasses. The murine La protein and the RNA binding subclass of calf thymus La protein showed ATPase/dATPase activity in the presence of DNA-RNA or RNA-RNA hybrids. A novel monoclonal anti-La antibody (La11G7) and patients' anti-La antibodies immunoadsorbed to homogeneously purified La protein were able to inhibit the enzyme activity of La protein. La protein was able to melt a synthetic DNA-RNA hybrid in a reaction that required ATP hydrolysis. The RNA binding ability of the nonbinding subclass was restored by treatment with sialidase. This treatment also restored the protein's ATP-dependent melting activity.
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PMID:Characterization of the autoantigen La as a nucleic acid-dependent ATPase/dATPase with melting properties. 168 13

The NTRC protein of enteric bacteria is an enhancer-binding protein that activates transcription in response to limitation of combined nitrogen. NTRC activates transcription by catalyzing formation of open complexes by RNA polymerase (sigma 54 holoenzyme form) in an ATP-dependent reaction. To catalyze open complex formation, NTRC must be phosphorylated. We show that phosphorylated NTRC has an ATPase activity, and we present biochemical and genetic evidence that NTRC must hydrolyze ATP to catalyze open complex formation. It is likely that all activators of sigma 54 holoenzyme have an ATPase activity.
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PMID:The phosphorylated form of the enhancer-binding protein NTRC has an ATPase activity that is essential for activation of transcription. 183 69

A putative ATPase gene was cloned from Trypanosoma brucei genomic DNA. The length of the gene open reading frame is 3,033 bp, predicting a protein of about 110 kDa. The sequence of this protein shares 10 blocks of homology with other eukaryotic ATPases, including the putative phosphorylation site characteristic of P-ATPases. Its hydropathy profile reveals 8-10 potential membrane-spanning regions. While the amino acid sequence of the T. brucei ATPase shows only 25% overall homology with its counterpart from the related kinetoplastid protozoan Leishmania donovani, 49% sequence conservation is found when compared with the calcium-ATPase from rabbit sarcoplasmic reticulum. This gene is present in only one copy, localized in the large chromosome fraction. It is transcribed at a similar level in procyclic and bloodstream forms, as a 4.3-kb mRNA. Run-on assays suggest continuous transcription of the gene and flanking sequences over at least 10 kb, by a RNA polymerase sensitive to alpha-amanitin. Transcription inhibition by UV irradiation suggests that the ATPase gene is more than 4 kb downstream from its promoter.
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PMID:Structure and transcription of a P-ATPase gene from Trypanosoma brucei. 183 43

A kinase activity specific for the C-terminal repeat domain (CTD) of RNA polymerase II is associated with nearly homogeneous yeast general initiation factor b by three criteria: cofractionation on the basis of size and charge and coinactivation by mild heat treatment. The kinase phosphorylates the CTD at multiple sites in a processive manner. Factor b may possess a DNA-dependent ATPase activity as well. Both kinase and DNA-dependent ATPase activities exhibit the same nucleotide requirements as previously demonstrated for the initiation of transcription. These results support the idea that phosphorylation of the CTD lies on the pathway of transcription initiation and identify a catalytic activity of a general factor essential for the initiation process.
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PMID:CTD kinase associated with yeast RNA polymerase II initiation factor b. 183 79

Vaccinia virus RNA polymerase requires the vaccinia early transcription factor, VETF, for the in vitro initiation of transcription at early gene promoters in a reaction requiring ATP hydrolysis. VETF binds specifically to early gene promoters and has an associated DNA-dependent ATPase activity. The effect of ATP on the interaction of VETF with the promoter for the vaccinia growth factor gene promoter has been examined. ATP had no marked effect on the steady-state level of promoter binding but dramatically affected the kinetics of dissociation of VETF from the promoter. The half-life of the VETF-promoter complex was greatly reduced in the presence of ATP. The destabilization of the complex was specific for ATP and dATP, consistent with the substrate specificity of the VETF-associated ATPase. ADP or the non-hydrolyzable ATP analog adenylyl-imidodiphosphate did not destabilize the complex suggesting that ATP hydrolysis is obligatory for dissociation. These findings provide a link between the promoter binding and ATPase activities associated with VETF and suggest that the ATP-dependent dissociation of the VETF-promoter complex is an important event in the transcription of vaccinia virus early genes.
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PMID:A role for ATP hydrolysis in vaccinia virus early gene transcription. Dissociation of the early transcription factor-promoter complex. 186 72

Two open reading frames on a 3.7-kb BglII-XbaI fragment which encodes the Staphylococcus aureus cadA cadmium (and zinc) resistance determinant of plasmid pI258 were identified (G. Nucifora, L. Chu, T. K. Misra, and S. Silver, Proc. Natl. Acad. Sci. USA 86:3544-3548, 1989). The [35S]methionine-labelled protein products of the 727-amino-acid CadA ATPase and of the 122-amino-acid CadC polypeptide in Escherichia coli were identified by using the T7 RNA polymerase-promoter expression system. A truncated CadA polypeptide (402 amino acids) did not confer resistance in S. aureus but was expressed in E. coli under control of the T7 RNA polymerase-promoter. Removal of 678 nucleotides from the 5' end of the published sequence (which includes the cadA promoter) abolished resistance to cadmium, whereas a 146-nucleotide-shorter deletion was without effect. The cadC gene is needed in addition to cadA for full resistance to cadmium in S. aureus and Bacillus subtilis. cadC functions both in cis and in trans.
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PMID:A second gene in the Staphylococcus aureus cadA cadmium resistance determinant of plasmid pI258. 193 59

Spinach chloroplast RNA polymerase has been shown to efficiently terminate transcription at the threonine attenuator (thra) from Escherichia coli. In this study, efficient transcription termination by the chloroplast RNA polymerase was observed at a second prokaryotic terminator, the histidine attenuator (hisa) from Salmonella typhimurium. Termination occurred regardless of the orientation of either attenuator. In higher-plant chloroplast DNA, the genes for the beta subunit of the ATPase (atpB) and the large subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase (rbcL) are adjacent and divergently transcribed. Bidirectional transcription vectors, containing the histidine and threonine terminators, were constructed to analyze the divergently oriented atpB and rbcL promotors. One plasmid construction, pRTT7, contained two tandem copies of the threonine attenuator (pRTT7). Two additional constructs, pRHT1 and pRHT2, each contained oppositely oriented copies of thra and hisa. A DNA fragment containing the rbcL and atpB promoters was inserted between the two terminators present in the pRTT7, pRHT1, and pRHT2 plasmids. Transcription of these recombinant DNAs by spinach chloroplast RNA polymerase resulted in discretely sized rbcL and atpB transcripts. In addition, these bidirectional transcription vectors were used to identify previously uncharacterized chloroplast promoters.
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PMID:Analysis of chloroplast promoters using bidirectional transcription vectors. 215 32


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