Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.6 (RNA polymerase)
 34,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have determined the nucleotide sequence of the rpoD gene which codes for the sigma subunit of RNA polymerase from E. coli K12. The gene, which we formerly cloned as a HindIII restriction fragment in the transducing phage, charon 25, was recloned into several plasmids. We have determined a 2600 base pair DNA sequence which includes the entire structural gene for sigma. The resulting amino acid sequence agrees with previous information obtained about sigma including the amino acid composition, partial sequence data for the N-terminus, the highly acidic nature of the polypeptide, and the cleavage pattern at cysteines. The molecular weight of 70,263 daltons calculated for the 613 amino acid polypeptides is significantly lower than had been determined previously by SDS polyacrylamide gel analysis.
 ...
PMID:The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12. 626 63

The nusA gene of Escherichia coli has been cloned into the plasmid vector pKC30 under the control of the inducible lambda pL promoter. When a strain carrying this plasmid is induced, NusA protein is overproduced more than 100-fold and constitutes 20-30% of the total cellular protein. The NusA protein purified from this strain appears identical to authentic NusA protein in its migration on SDS polyacrylamide gels and on isoelectric focusing gels. It is also able to function properly in in vitro termination and antitermination assays and in its ability to bind to E. coli core RNA polymerase.
 ...
PMID:Overproduction of Escherichia coli NusA protein. 632 50

mRNA guanylyltransferase has been extensively purified from calf thymus. A GTP-binding assay was used based on the observations by Shuman and Hurwitz (1981) and Venkatesan and Moss (1982) that vaccinia virus and HeLa cell mRNA guanylyltransferases bind the GMP moiety from GTP in the absence of an acceptor RNA. The mol. wt. of the purified enzyme from calf thymus, estimated by polyacrylamide gel electrophoresis in the presence of SDS, is 65 000. The major protein in the purified enzyme fraction comigrates with the peptide labelled with GMP. Based on scans of silver-stained polyacrylamide gels, mRNA guanylyltransferase constitutes greater than 50% of the protein in these fractions. The enzyme catalyzed the guanylylation at the 5' end of poly(A) with a mixture of diphosphate and triphosphate ends. No evidence was obtained for a direct interaction between mRNA guanylyltransferase and RNA polymerase B (II).
 ...
PMID:Purification of mRNA guanylyltransferase from calf thymus. 632 86

The T4 mot gene regulates middle mode RNA synthesis in phage-infected cells. The mot gene product has been identified in two ways. (i) Infections with amber and temperature-sensitive mot mutants both lead to the disappearance of a number of protein bands on SDS-polyacrylamide gels. These are middle mode proteins whose synthesis depends on mot function. The mot protein disappears from such gels after infection with a mot amber mutant, but not with the mot missense mutant. (ii) This same protein is the only one to have a charge alteration when proteins from wild-type phage and mot missense mutant infections are compared by two-dimensional gel electrophoresis. Mot protein is basic and has a mol. wt. of 24 000. It migrates between the positions of gp 1 and gp IPIII on 15% SDS-polyacrylamide gels. Mot protein synthesis begins immediately after infection and continues until 4 min after infection at 30 degrees C, after which time it is strongly inhibited. This inhibition depends neither on T4 DNA synthesis nor on ADP ribosylation of the alpha subunits of the Escherichia coli RNA polymerase. The mot protein does not regulate its own biosynthesis. It is stable throughout the course of infection.
 ...
PMID:Identification and biosynthesis of the bacteriophage T4 mot regulatory protein. 635 9

A chicken liver non-histone protein fraction repressing DNA transcription in vitro was isolated using ultrasound shearing followed by precipitation with divalent cations. It was characterized by SDS-polyacrylamide electrophoresis and isoelectric focusing. This inhibitory protein fraction showed strong affinity to DNA and represented non-histone proteins with main bands of mol. wt about 35000 and 56000 and isoelectric points about 5.7 and 6.2. The inhibitory non-histone protein fraction seems to repress DNA transcription by interacting with DNA template rather than with RNA polymerase.
 ...
PMID:Chicken liver non-histone protein fraction repressing DNA transcription in vitro. 647 55

RNA nucleotidyltransferase (EC 2.7.7.6) of Streptomyces granaticolor was purified by precipitation with polymin P and ammonium sulphate, affinity chromatography on DNA- cellulose and gell filtration on Biogel A 1.5 m. SDS-polyacrylamide gel electrophoresis revealed 8 protein bands of molar mass ranging from 37 to 130 kg/mol. Proteins of molar mass of 130 and 120 kg/mol were identified to be beta and beta subunits, respectively. The role of other subunits of the enzyme is discussed.
 ...
PMID:Purification of DNA-dependent RNA polymerase from Streptomyces granaticolor. 664 21

The DNA binding subunits of RNA polymerase II from Ehrlich ascites tumor cells were investigated in the following three ways. (1) RNA polymerase II was dissociated in urea and the binding of the dissociated subunits to DNA was investigated. (2) The RNA polymerase II: DNA complex was dissociated progressively with various concentrations of urea, and the subunits firmly attached to DNA were investigated. (3) RNA polymerase II was dissociated into subunits in a SDS-polyacrylamide gel containing urea and blotted onto a nitrocellulose filter. The filter was then incubated with 32P-nick-translated DNA to identify the DNA binding subunits. These procedures all showed that the largest subunit a of RNA polymerase II had strong affinity to DNA. It was found that a portion of subunits b and c could be recovered in DNA fraction when analyzed by procedures (1) and (2), but no significant DNA binding activity was detected when analyzed by procedure (3), suggesting that these subunits have either a much weaker affinity toward DNA compared to a or have affinity to a itself.
 ...
PMID:Identification of the DNA binding subunit of RNA polymerase II from Ehrlich ascites tumor cells. 668 76

The relative rates of RNA polymerase biosynthesis in Bacillus subtilis has been examined under steady-state growth conditions. The synthesis of RNA polymerase subunits (alpha, beta, beta', omega) has been followed by subunit fractionation of immunoprecipitated [3H]-labelled samples on SDS-polyacrylamide gels. The stoichiometries of alpha:beta:beta':omega subunits have been determined from cultures pulse-labelled during steady-state growth. The results suggest that an unassembled pool of the alpha-subunit exists from which the holoenzyme is formed. Upon shift-up from acetate to glycerol containing medium, a rapid rise in the differential rate of core enzyme synthesis was observed, while the rate of synthesis of the alpha-subunit was not stimulated. During shift-down, a concomitant reduction in the rate of synthesis of all subunits occurred for the first 20 min after the shift; thereafter, a rate of synthesis characteristic of the new growth rate was established. As cultures enter sporulation, an immediate reduction in the rate of beta beta'-subunit synthesis was demonstrated.
 ...
PMID:RNA polymerase subunit biosynthesis in Bacillus subtilis. 680 67

Two paramyxovirus isolates recovered from the peripheral blood leukocytes of a patient with subacute sclerosing panencephalitis were characterized by biological, immunological, and molecular techniques. Both virus isolates possessed neuraminidase activity but demonstrated reduced hemagglutination potential. Neutralization titrations showed that the viruses were clearly related to, but were distinct from, simian virus 5. Characterization of purified virus preparations by SDS-PAGE showed that the structural polypeptides of the viruses were similar to those of simian virus 5, but distinct differences were noted as well. In addition, the virus isolates were found to differ from one another, particularly with regard to the major putative transcriptase protein (L).
 ...
PMID:Characterization of nonmeasles paramyxovirus isolates from a patient with subacute sclerosing panencephalitis. 733 93

Treatment of isolated nucleoli with Sarkosyl (2%) dissociated 99.5% of the proteins. The residual DNA-protein complex contained the endogenous transcriptional activity which had a high fidelity of RNA synthesis. Electron microscopic analysis of this residue fraction showed the presence of 150-200A diameter protein globules present along the length of some of the DNA fibers. SDS-polyacrylamide gel electrophoretic analysis of the proteins of the complex indicated that the subunits of purified RNA polymerase I were only a minor component of this complex. Associated with the complex were the U3 and 5S RNA.
 ...
PMID:Characterization of a nucleolar residue fraction that specifically transcribes preribosomal RNA. 743 25


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>