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)

Human mitochondrial transcription factor 1 (mtTF1) has been sequenced and is a nucleus-encoded DNA binding protein of 204 amino acids (24,400 daltons). Expression of human mtTF1 in bacteria yields a protein with correct physical properties and the ability to activate mitochondrial DNA promoters. Analysis of the protein's sequence reveals no similarities to any other DNA binding proteins except for the existence of two domains that are characteristic of high mobility group (HMG) proteins. Human mtTF1 is most closely related to a DNA binding HMG-box region in hUBF, a human protein known to be important for transcription by RNA polymerase I.
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PMID:Similarity of human mitochondrial transcription factor 1 to high mobility group proteins. 203 27

The binding of DNA binding protein HMG1 to palindromic sequences that can form the cruciform structure in supercoiled DNA and the subsequent effects on the transcription of the sequence were examined. The results show that the cruciform structure formed under negative supercoiling is a block to transcription and that HMG1, which bound selectively to single-stranded region within the cruciform, can remove the block by altering DNA conformation to allow the stalled RNA polymerase at the block to resume transcription.
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PMID:The selective binding of HMG1 to the cruciform DNA structure and the subsequent resumption of transcription. 210 22

Various agents were tested for their effects on microbial proteases, which activity was monitored by the analysis of cleaved peptide bands in SDS-polyacrylamide gel electrophoresis. Using casein as a substrate, fungal protease (type XIX) was inhibited by the phenyl methyl sulphonyl fluoride, chymostatin, antipain and leupeptin, while bacterial protease (type XXVI) was inhibited by phosphatidyl glycerol, phosphatidyl inositol and sphingosine. MS2 RNA exerted minor inhibition on the bacterial proteolysis of regulatory subunits of cyclic AMP-dependent protein kinase (A-PK). The cleavage of DNA binding protein by both proteases was inhibited, in the presence of MS2 RNA and lambda DNA. In comparison, phosphatidyl serine slightly stimulated the fungal protease on the cleavage of ribonuclease T1. RNA polymerase is a good substrate of the bacterial protease as indicated by the generation of multiple cleaved peptide fragments, whereas alkaline phosphatase is not susceptible to proteolysis.
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PMID:A further study on the regulation of microbial proteases. 222 36

The rpoH (htpR) gene of Escherichia coli encodes a sigma factor which confers upon RNA polymerase the ability to recognize the promoters for genes responsive to the phenomenon termed the heat shock response. dnaA protein, a sequence-specific DNA binding protein, is required for initiation of chromosomal replication by binding to sites within the chromosomal origin. dnaA protein also autoregulates its expression by binding to a site in the dnaA promoter region. Two copies of the dnaA protein recognition sequence are present within the rpoH promoter region. Using filter binding assays, dnaA protein was observed to bind specifically to DNA fragments containing the rpoH promoter region with greater affinity than its binding to the dnaA promoter region. By contrast, reduced binding to a DNA fragment containing the lacUV5 promoter was observed. DNase I footprint analysis indicated that dnaA protein protected specific sites within the rpoH promoter region. The binding of dnaA protein to the rpoH promoter region resulted in transcriptional repression from two of the three promoters of the rpoH gene in vitro. Elevated levels of dnaA protein repressed transcription from these two rpoH promoters in vivo. These results indicate that dnaA protein regulates rpoH transcription to influence the expression of genes under rpoH control.
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PMID:dnaA protein regulates transcriptions of the rpoH gene of Escherichia coli. 254 Jan 87

The binding to supercoiled plasmid DNA as well as to double-stranded short DNA fragments of the DNA binding protein. ASBIII, from S. hygroscopicus has been demonstrated by gel retardation asay. As further revealed by sedimentation analysis, the protein-DNA complex formation also involves condensation of DNA and an aggregation step at higher total protein-to-DNA ratio (w/w). In vitro studies of the transcriptional activity of DNA-protein complexes showed that the ASBIII protein inhibits the overall template activity in the RNA polymerase II system to nearly similar extents for various DNA's. Preincubation of ASBIII-DNA complexes of different GC content, however, suggested a selective inhibitory effect on GC-rich DNA due to the higher stability of this complex. The results also indicate that the initiation of transcription of the GC-rich DNA template is affected by the ASBIII protein. The present results on the DNA binding properties and inactivation of the transcription of the ASBIII protein suggest that this protein may be a potential candidate for the local compaction of chromosomal DNA in Streptomyces hygroscopicus.
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PMID:DNA binding protein from Streptomyces hygroscopicus: detection of binding by gel retardation, sedimentation and effects on the transcriptional activity in vitro. 255 24

Sp1 is a sequence-specific DNA binding protein that activates RNA polymerase II transcription from promoters that contain properly positioned GC boxes. A series of deletion mutants of Sp1 were expressed in Escherichia coli and used to identify separate regions of the protein that are important for three different biochemical activities. The sequence-specificity of DNA binding was conferred by Zn(II) fingers, whereas a different region of Sp1 appeared to regulate the affinity of DNA binding. The E. coli-synthesized Sp1 was able to stimulate initiation of RNA synthesis in vitro, and at least two distinct segments of the protein contributed to its transcriptional activity.
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PMID:Distinct regions of Sp1 modulate DNA binding and transcriptional activation. 305 95

Nuclear Factor I (NF1) is a DNA binding protein that is known to function in the replication of Adeno virus and also binds to many promoters recognized by RNA polymerase II. We have found that there is also an NF1 binding site within the ribosomal gene promoter from Xenopus laevis as well as in several other promoters recognized by RNA polymerase I. The function of a binding site for a polymerase II transcription factor within a promoter recognized by polymerase I is not known. However, its presence suggests interesting regulatory possibilities.
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PMID:The Xenopus laevis ribosomal gene promoter contains a binding site for nuclear factor-1. 320 19

The human ribosomal RNA promoter contains two distinct control elements (UCE and core) both of which are recognized by the sequence-specific DNA binding protein UBF1, which has now been purified to apparent homogeneity. The purified factor activates RNA polymerase I (RNA pol I) transcription through direct interactions with either control element. A second RNA pol I transcription factor, designated SL1, participates in the promoter recognition process and is required to reconstitute transcription in vitro. Although SL1 alone has no sequence-specific DNA binding activity, deoxyribonuclease I footprinting experiments reveal that a cooperative interaction between UBF1 and SL1 leads to the formation of a new protein-DNA complex at the UCE and core elements. In vitro transcription experiments indicate that formation of the UBF1-SL1 complex is vital for transcriptional activation by UBF1. Thus, protein-protein interactions between UBF1 and SL1 are required for targeting of SL1 to cis-control sequences of the promoter.
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PMID:Functional cooperativity between transcription factors UBF1 and SL1 mediates human ribosomal RNA synthesis. 341 83

Facilitated diffusion accounts for the rapid rate of association of many bacterial DNA binding proteins with specific DNA sequences in vitro. In this mechanism the proteins bind at random to non-specific sites on the DAN and diffuse (by 'sliding' or 'hopping') along the DNA chain until they arrive at their specific functional sites. We have investigated whether such a mechanism can operate in chromatin by using a bacterial DNA binding protein, Escherichia coli RNA polymerase, that depends on linear diffusion to locate initiation sites on DNA. We have measured the competition between chromatin and its free DNA for the formation of initiation complexes. Only the short linker segments exposed by the removal of histone H1 are available for interaction with the polymerase, but the sparsely distributed promoter sites on the linker DNA of such a polynucleosome chain are located at the same rate as those on DNA. We conclude that the polymerase is free to migrate between the separate linker DNA segments of a polynucleosome chain to reach a promoter site. This chain thus permits the 'hopping' of proteins between neighboring linker segments in their search for a target site on the accessible DNA.
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PMID:Facilitated diffusion of a DNA binding protein on chromatin. 354 17

A soluble enzyme system has been prepared from a phage P4-infected Escherichia coli strain that supports the replication of exogenous, supercoiled P4 DNA. This DNA synthesis in vitro depends upon the four deoxyribonucleotides and ATP, but is enhanced about four- to fivefold by the presence of other ribonucleotides. E. coli DNA polymerase III holoenzyme, the E. coli single-strand DNA binding protein, and the partially purified P4 alpha gene product are required for replication in vitro. Rifamycin does not inhibit P4 replication in vitro. Since the P4 alpha gene codes for a rifamycin-resistant RNA polymerase (Barrett et al., 1983), and since P4 DNA replication is independent of the host primase (Bowden et al., 1975), we believe the alpha gene product is functioning as a P4-specific DNA primase.
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PMID:The replication of bacteriophage P4 DNA in vitro. Partial purification of the P4 alpha gene product. 387 88


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