Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P51532 (transcriptional activator)
 6,546 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The nahR gene from the NAH7 naphthalene degradation plasmid encodes a LysR-type transcriptional activator of the nah and sal promoters (Pnah and Psal, respectively) that responds to the inducer salicylate. In vivo methylation protection experiments with dimethyl sulfate showed that in the absence of inducer, NahR interacts in a similar manner with its target sites at Psal and Pnah. Both target sites also have very similar sequences comprised of a 4-base pair interrupted dyad containing two symmetrical guanines (-73 and -64 of Pnah; -71 and -62 of Psal), each located in adjacent major grooves on the same helical face, and both strongly protected by NahR. When inducer was present, several additional guanines of Pnah (-35, -45, and -58) and Psal (-42 and -40) became protected from methylation, while a guanine at -52 of Pnah became markedly enhanced for methylation, indicating that inducer and NahR-dependent interactions with these downstream sites of each promoter are quite different. Deletion of Psal sequences downstream of -30 did not affect its methylation patterns suggesting that NahR alone is responsible for the altered reactivities of these nucleotides. Similar in vivo methylation analyses with inducer-insensitive or inducer-independent NahR mutants also suggested that all alterations in methylation sensitivity are directly caused by NahR. It is more probable that the salicylate-induced reactivity changes result from direct NahR-guanine contacts which are required for, but not sufficient for transcription activation; however, they could also result from NahR-induced DNA contortions caused by upstream protein-DNA contacts.
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PMID:In vivo interactions of the NahR transcriptional activator with its target sequences. Inducer-mediated changes resulting in transcription activation. 204 Jun 3

Primer-extension analysis of the Klebsiella pneumoniae nifH promoter was used to determine changes in the accessibility of the promoter DNA to methylation after exposure of growing cells to dimethyl sulfate. Four guanine residues present in the nifH upstream activator sequence (UAS), the proposed NifA binding site, were protected from methylation and two guanine residues were hypermethylated when the transcriptional activator protein NifA was present in the cells. The interaction detected at the nifH UAS was independent of the alternative sigma factor NtrA required for transcription of the nifH and other nif promoters. Mutations within the nifH UAS that diminish NifA-dependent transcriptional activation reduced the interaction at the UAS. It seems likely that the pattern of methylation protection observed in the nifH UAS is the result of NifA binding.
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PMID:NifA-dependent in vivo protection demonstrates that the upstream activator sequence of nif promoters is a protein binding site. 284 2

By in vivo DMS footprint and reporter gene analyses we identified two transcription factor binding sites in the human c-sis/PDGF B gene promoter. The low basal activity of the PDGF B promoter in HeLa and undifferentiated K562 cells, which express low PDGF B mRNA levels, and in PC3 cells, which express a high PDGF B mRNA level, results from binding of a weak transcriptional activator between positions -64 and -61 relative to the transcription start site. Cytotrophoblast-like JEG-3 cells, which do not express the 3.5 kb PDGF B mRNA, contain a transcriptional activator directed at the -64/-61 sequence, but DNA methylation may render the endogenous promoter inaccessible to this activator. A CCACCCAC element at position -61/-54 was identified as the in vivo binding site for a strong transcriptional activator in phorbol ester-treated megakaryocytic K562 cells, which express a high PDGF B mRNA level. Primary human fibroblasts, which do not transcribe the PDGF B gene, contain a transcriptional activator that recognizes an element between positions -60 and -45 but does not bind to the endogenous unmethylated promoter. Our results show that the complex expression pattern of the human PDGF B gene involves the cell type-specific expression of weak and strong transcriptional activators and regulation of promoter accessibility to these factors.
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PMID:In vivo footprinting and functional analysis of the human c-sis/PDGF B gene promoter provides evidence for two binding sites for transcriptional activators. 773 90

The E. coli rrnB P1 promoter owes its strength, in part, to the transcriptional activator protein FIS. FIS binds to three sites upstream of the RNA polymerase (RNAP) binding site and increases transcription in vivo four to ten-fold. In this report, hydroxyl radical and DMS footprinting analyses show that FIS binds to its three sites along one side of the DNA helix, and that FIS bound at the promoter-proximal site (site I) and RNAP bound at the promoter are in close proximity. The binding of FIS at site I and RNAP at the promoter are mutually cooperative. These observations support a model for direct interaction between the FIS protein bound at site I and RNAP in transcription activation at rrnB P1. We also find that FIS does not bind cooperatively to its three sites upstream of rrnB P1, and that the relatively small activation associated with FIS bound at sites II and III does not result indirectly by facilitation of binding of FIS to site I.
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PMID:The transcriptional activator protein FIS: DNA interactions and cooperative interactions with RNA polymerase at the Escherichia coli rrnB P1 promoter. 784 12

In this report a modification to the in vivo footprinting assay is described. The method includes dimethyl sulfate treatment of whole yeast cells, followed by reiterative primer extension of the methylated genomic DNA using Taq DNA polymerase. Under appropriate reaction conditions chain extension terminates opposite a methylated purine when Taq DNA polymerase encounters a modified adenine or guanine. The procedure was used to examine, in vivo DNA-protein contacts over the upstream activation site (UAS) of the Saccharomyces cerevisiae PYK gene. In vivo analysis, using isogenic strains of yeast and Escherichia coli transformed with plasmid DNAs, confirmed the binding of both the trans-acting factor RAP1 and the transcriptional activator GCR1 to cis-acting recognition sites located within the PYK UAS element.
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PMID:A simple in vivo footprinting method to examine DNA-protein interactions over the yeast PYK UAS element. 819 Jun 36

MalT, the transcriptional activator of the Escherichia coli maltose regulon, is a 901-amino acid-long protein that specifically binds to short, asymmetric nucleotide sequences present in several copies in the promoters of the regulon. We report that the protein structure involved in this specific binding is carried by a small C-terminal part of MalT encompassing the last 95 amino acid residues. This was demonstrated by fusing the last 95 codons of malT to the gene that encodes glutathione S-transferase, purifying the hybrid protein by affinity chromatography, and comparing the DNase I and dimethyl sulfate footprints of the hybrid and of wild-type MalT on different MalT-binding sites. MalT belongs to a large family of prokaryotic transcriptional activators, which share significant homology in their approximately 60-amino acid C-terminal regions. Our result strongly supports the suggestion that the region of homology corresponds to the DNA-binding domain of the proteins in this family.
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PMID:A small C-terminal region of the Escherichia coli MalT protein contains the DNA-binding domain. 822 7

The contributions from the secondary structure of the transcriptional activator protein C of bacteriophage Mu to its specific DNA binding and the influence of various factors, viz., electrolytes, and minor groove and major groove binders on this protein-DNA interaction have been addressed. Circular dichroism (CD) spectral results suggest that, in the absence of Mg2+, C protein exhibits a beta-pleated sheetlike structure and Mg2+ changes the conformation to a more alpha-helical structure which could provide specific geometrical constraints complementary to those of DNA-helix. Thus, Mg2+ acts as a cofactor for the binding of the C protein to its specific site in DNA by inducing conformational changes in the protein. Competitive binding studies with minor and major groove binding drugs, viz., distamycin A and methyl green, respectively, and the DMS footprinting data indicate that the C protein recognizes the major groove of DNA during complex formation. Further, upon major groove binding, C protein brings about changes in DNA conformation; such conformational changes could have implications in the transcription process.
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PMID:Mg2+ mediated sequence-specific binding of transcriptional activator protein C of bacteriophage Mu to DNA. 952 3

The bacteriophage Mu mom gene encodes the unique DNA-modification function of the phage. Regulation of the mom gene at the transcriptional level is brought about by the transactivator protein C of the phage. The mom promoter is an activator-dependent weak promoter having poor -10 and -35 elements separated by a 19 bp suboptimal spacer region. These features could constrain RNA polymerase occupancy at the promoter. Here, we have probed into the mechanism by which C protein acts as a transcriptional activator at Pmom. In vivo dimethyl sulfate footprinting studies demonstrate C protein-mediated asymmetric distortion of its specific site at the mom regulatory region. Using a coupled topoisomerase assay, we demonstrate that C protein induces the unwinding of DNA. This C-mediated unwinding seems to be localised to the 3' flanking region of the C binding site located adjacent to and overlapping the -35 element of Pmom. These results suggest that C protein-mediated torsional changes could be reorienting the -10 and -35 elements to a favorable conformation for RNA polymerase occupancy at the mom promoter.
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PMID:Transcriptional activator C protein-mediated unwinding of DNA as a possible mechanism for mom gene activation. 983 13