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)

Transcripts from the rplKAJL-rpoBC ribosomal protein-RNA polymerase gene cluster have been quantified and their ends mapped using RNA-DNA hybridization, sucrose density-gradient sedimentation, Northern hybridization and S1 nuclease protection. The results indicate that the most abundant transcript is the 2600 nucleotide tetracistronic L11-L1-L10-L12 mRNA initiated at the upstream major PL11 promoter and terminated at the transcription attenuator in the L12-beta intergenic space. Somewhat less abundant 1300 nucleotide L11-L1 and L10-L12 bicistronic transcripts were observed. The 3' ends of the L11-L1 transcripts were heterogeneous; most of the ends were localized to three sites within a 110 base-pair region in the L1-L10 intergenic space. This intergenic space encodes also the major PL10 promoter and the mRNA binding site for the L10 translational control protein. Two 5' ends were observed for L10-L12 bicistronic mRNA, one at the PL10 promoter and the other 150 nucleotides further downstream in a region in which promoter activity has not been detected. It is suggested that this second downstream 5' end is generated by processing of the transcripts initiated at the major PL10 promoter. No transcript initiation in the L10-L12 intergenic space was detected. About 80% of the transcripts reading through the L12 gene were terminated in the vicinity of the transcription attenuator that is responsible for the reduction in the expression of the downstream RNA polymerase genes. Transcripts reading through the attenuator were partially processed by RNase III within a potential hairpin structure in the RNA transcript. Processing appears to produce 3' and 5' transcript end sites separated by about ten nucleotides. No other major 5' ends were observed in the L12-beta intergenic space. These results indicate that the two major promoters, PL11 and PL10, are both utilized to drive the interrelated transcriptional expression of this ribosomal protein-RNA polymerase gene cluster.
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PMID:Transcription products from the rplKAJL-rpoBC gene cluster. 244 6

cDNA clones encoding three antigenically related human ribosomal phosphoproteins (P-proteins) P0, P1, and P2 were isolated and sequenced. P1 and P2 are analogous to Escherichia coli ribosomal protein L7/L12, and P0 is likely to be an analog of L10. The three proteins have a nearly identical carboxy-terminal 17-amino-acid sequence (KEESEESD(D/E)DMGFGLFD-COOH) that is the basis of their immunological cross-reactivity. The identities of the P1 and P2 cDNAs were confirmed by the strong similarities of their encoded amino acid sequences to published primary structures of the homologous rat, brine shrimp, and Saccharomyces cerevisiae proteins. The P0 cDNA was initially identified by translation of hybrid-selected mRNA and immunoprecipitation of the products. To demonstrate that the coding sequences are full length, the P0, P1, and P2 cDNAs were transcribed in vitro by bacteriophage T7 RNA polymerase and the resulting mRNAs were translated in vitro. The synthetic P0, P1, and P2 proteins were serologically and electrophoretically identical to P-proteins extracted from HeLa cells. These synthetic P-proteins were incorporated into 60S but not 40S ribosomes and also assembled into a complex similar to that described for E. coli L7/L12 and L10.
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PMID:Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. 332 86

E. coli DNA fragment containing the rpoB gene with an rpoB3 rifampicin resistance dominant mutation (coding for the beta-subunit of RNA polymerase), genes rpI J and rpI L coding for the ribosomal proteins L7/L12 and L10, and promoters determining transcription of all these genes were cloned in M13mp8 and WB2348 filamentous phages. E. coli cells containing recombinant phages acquired resistance to rifampicin up to its 600 micrograms/ml concentration. When cloned into M13mp8 and WB2348 phages, the given fragment is oriented in such a way that the direction of the transcription initiated from its own promoter coincides with that initiated from the lac UV5 promoter. In both cases the recombinant phages have no stable rifampicin resistance which is coded by the fragment.
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PMID:[Unidirectional orientation of the rpo B gene of E. coli cloned into filamentous M13mp8 and M13WB2348 phages]. 609 81

Plasmids pNF1337 and pNF1341, which contain part of the L10 operon including the RNA polymerase beta-subunit gene, have been used as templates in vitro to investigate expression of the beta-subunit gene. For these studies, the synthesis of the first dipeptide of the beta subunit, fMet-Val, was measured instead of that of the entire protein. By using this dipeptide system, we studied the effects of RNA polymerase holoenzyme and L factor (nus A gene product) on fMET-Val synthesis and compared the relative effects of the primary and secondary promoters in the L10 operon on expression of the beta-subunit gene. The results show that the inhibitory effect of RNA polymerase on beta-subunit synthesis and the stimulatory effect of L factor occur before formation of the first dipeptide bond. In this in vitro system, the secondary promoters account for about 50% of the total fMet-Val synthesized. Although the primary promoter is sensitive to guanosine 5'-diphosphate 3'-diphosphate in vitro, the secondary promoters are not affected by this nucleotide.
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PMID:In vitro synthesis of the first dipeptide of the beta subunit of Escherichia coli RNA polymerase. 628 8

The genes encoding the beta and beta' subunits of RNA polymerase in E.coli, rpoB and rpoC, lie downstream of at least two ribosomal protein genes, rplJ (encoding L10) and rplL (L7/12), in a common operon. All four genes are served by promoter PL10, and an attenuator (partial terminator) of transcription, t1, lies between rplJL and rpoBC. Treatment of E.coli with rifampicin, under conditions producing partial inhibition of general RNA synthesis, can stimulate transcription of rpoBC. We have investigated the locus of this effect by fusing PL10 and t1 separately to galK, in suitable plasmids. Our studies of these fusions, and similar fusions involving transcriptional terminators derived from coliphage T7, indicate that low concentrations of rifampicin cause increased readthrough of several different transcriptional terminators in E.coli in vivo, including rpo t1. We discuss whether or not this unspecific mechanism is solely responsible for the observed stimulatory effects of the drug on rpoBC transcription.
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PMID:Evidence that rifampicin can stimulate readthrough of transcriptional terminators in Escherichia coli, including the attenuator of the rpoBC operon. 629 75

The 319 nucleotide long intergenic region between the rplL (L12) and the rpoB (beta) genes of the L10 operon contains a transcription attenuation sequence and a RNase III mRNA processing sequence. Four site specific deletions located within this intergenic space which remove either the transcription attenuation sequence or the RNase III mRNA processing sequence or both sequences have been isolated on recombinant DNA plasmids carrying this operon. Deletions of sequences surrounding the RNase III processing site result in a uniform 80-90% reduction in the translational efficiency of beta subunit mRNA. This reduction in translation efficiency appears not to be related to processing per se; transcription of the rpoB and rpoC genes and the translation efficiency of the respective mRNA sequences were indistinguishable in an RNase III processing defective mutant (rnc) and its isogenic parent (rnc+). Deletions of the attenuator sequence result in a substantial increase in the downstream transcription of the beta subunit gene. The translational efficiency of RNase III processed beta subunit mRNA was found to be related in an inverse manner to the level of beta subunit synthesis. These result suggest that sequences on the mRNA in the vicinity of the RNase III processing site (i) are essential for efficient translation of beta subunit mRNA and (ii) are utilized for reducing the translational efficiency of the beta subunit mRNA when the beta subunit protein is produced in excess of that required for RNA polymerase assembly.
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PMID:Site specific deletions of regulatory sequences in a ribosomal protein-RNA polymerase operon in Escherichia coli. Effects on beta and beta' gene expression. 632 99

Using the in vitro mixed transcription system (Kajitani, M., and Ishihama, A. (1983) Nucleic Acids Res. 11, 671-686; Kajitani, M., and Ishihama, A. (1983) Nucleic Acids Res., 11, 3873-3889) we examined the effect of guanosine 3'-diphosphate, 5'-diphosphate (ppGpp), the chemical mediator of stringent control, on transcription of various Escherichia coli DNA fragments, each carrying a single specific promoter. We found that ppGpp inhibits transcription of stringently controlled genes, rrnE, rpsA, and rplJ, coding for ribosomal RNA, ribosomal protein S1 and L10, respectively, but not that of trp (tryptophan) and lacUV5 (lactose) genes. Among the multiple promoters of the rrnE and rpsA operons, the upstream promoters, rrnEp1 and rpsAp1, are subject to repression by ppGpp but the downstream promoters, rrnEp2 and rpsAp3, are insensitive. Taking these facts and the intrinsic strength of the respective promoters together, we suggest that the multiple promoters within the single and same operons play different physiological roles and are regulated by independent mechanisms. The inhibition by ppGpp takes place even after formation of open complexes, suggesting that the RNA polymerase bound to the sensitive promoters is accessible for interaction with ppGpp leading to rapid decay of the open complexes. During this study, we noticed that some promoters including recAp are activated in the presence of ppGpp, raising a possibility that ppGpp has dual effects on the promoter function.
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PMID:Promoter selectivity of Escherichia coli RNA polymerase. Differential stringent control of the multiple promoters from ribosomal RNA and protein operons. 636 18

Amber mutations in the rpoB gene specifying the beta subunit of RNA polymerase coupled with conditional amber suppressors were used to restrict the synthesis of core RNA polymerase in strains of Escherichia coli. Such a restriction stimulated transcription of genetic units containing RNA polymerase subunit genes. Within the L10 transcription unit (genetic structure: promotor (PL10), rplJ (L10), rplL (L7/L12), attenuator, rpoB (beta), rpoC (beta'), terminator), the initiation of transcription at the promotor was enhanced and termination at the transcription attenuator was relaxed. Transcription of the genetic unit containing the rpoA gene (alpha) was also enhanced. In the strain containing a non-polar amber mutation, the synthesis rate of the beta' subunit protein during the restriction correlated with the level of transcription of the beta and beta' genes. In contrast, synthesis of L7/L12 ribosomal protein remained essentially unaltered in spite of the elevated levels of L10-L7/L12 mRNA.
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PMID:Regulation of RNA polymerase synthesis. Conditional lethal amber mutations in the beta subunit gene. 698 28

The in vitro synthesis of Escherichia coli ribosomal proteins, L10 and L7/12, is specifically repressed by the addition of the L10-L7/12 complex, while that of other ribosomal proteins encoded by the neighboring operons is not affected. Thus the expression of the rpoBC operon is controlled by two autorepression systems, one for the two ribosomal proteins and the other for RNA polymerase beta and beta' subunits, both operating probably at the translational level.
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PMID:Autogenous regulation of the synthesis of ribosomal proteins, L10 and L7/12, in Escherichia coli. 699 49

The DNA-dependent in vitro synthesis of Escherichia coli ribosomal protein L10 was inhibited when L10 was added to the protein-synthesizing incubations. Addition of L10 had little or no effect on the synthesis of ribosomal protein L12, elongation factor Tu (tufB), or the beta and beta' subunits of RNA polymerase. In addition, ribosomal protein L12 did not inhibit its own synthesis or the synthesis of L10. Experiments using a mRNA-directed system showed that the inhibition of the synthesis of L10 by itself is at the level of translation of protein synthesis. The mechanism of inhibition does not appear to be due to increased degradation of L10 mRNA.
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PMID:Autogenous control of Escherichia coli ribosomal protein L10 synthesis in vitro. 699 2


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