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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 sequence of two new IS2 alleles with promoter activity (IS2-43 and IS2-44) is reported. The alleles are identical and are formed by a 17 bp tandem duplication in an AT-rich region of IS2. This created a new
RNA polymerase
binding site. A mutation was found that increased the frequency of formation of these 17 bp duplications but not of another class of duplications, the "mini-insertions". This suggested that the mechanisms of formation of the two classes of duplications are different.
Mol
Gen
Genet 1979 Aug
PMID:IS2-43 and IS2-44: new alleles of the insertion sequence IS2 which have promoter activity. 39 Mar 7
DNA-dependent RNA polymerase
has been found to be preferentially released at 43 degrees C from the folded nucleoids of an E. coli dnaAts mutant when compared with the same nucleoids at 30 degrees C or with nucleoids of a dnaA+ strain at either 30 degrees or 43 degrees C. The polypeptides released are identical in molecular weight with those of the beta and beta' constituent polypeptides of the core enzyme of a known E. coli
RNA polymerase
. In addition, these polypeptides are precipitated by specific anti-
RNA polymerase
rabbit IgG. The implications of the interactions of
RNA polymerase
with the dnaA gene product are discussed.
Mol
Gen
Genet 1979 Sep
PMID:Temperature dependent release of beta-beta' subunits of DNA dependent RNA polymerase from the folded chromosome of a dnaAts mutant of Escherichia coli. 39 Mar 10
We have analyzed some chemical properties of the sigma subunit of
RNA polymerase
from the sigma mutants: rpoD1 (Gross et al., 1978), rpoD2 (formerly known as alt-1) (Silverstone et al., 1972; Travers et al., 1978), and rpoD800 (Gross et al., 1979). Each of the three mutants is located at about 66 min on the E. coli genetic map and exhibits an alteration in the enzymatic properties of its sigma subunit. The tryptic peptides and isoelectric focusing behavior were analyzed for mutant and wild type sigma. A single, but different altered lysine tryptic peptide was observed for each mutant. No altered arginine tryptic peptides were observed. The rpoD800 mutant sigma showed an altered isoelectric point. These studies provide chemical evidence that the sigma polypeptide in all three mutants is altered and strongly support the conclusion that the mutations are in the structural gene for sigma.
Mol
Gen
Genet 1979 Oct 01
PMID:Altered chemical properties in three mutants of E. coli RNA polymerase sigma subunit. 39 26
Synthesis of DNA complementary to the transferred strand of an IncI alpha plasmid has been shown previously to require DNA polymerase III. The possible involvement of the two defined priming proteins of Escherichia coli K12,
RNA polymerase
and primase, in initiating this conjugal DNA synthesis had been examined. Primase was inactivated using temperature-sensitive dnaG3 mutants and
RNA polymerase
was inhibited using rifampicin. When these two proteins were simultaneously inactivated in both parental strains, the average recipient synthesised at least one single-stranded equivalent of R144drd-3 before the rifampicin-treated donors lost the ability to transmit DNA. It is proposed that the product of a plasmid transfer gene is responsible for initiating this DNA synthesis in recipients. The results imply that this protein is supplied by the donors.
Mol
Gen
Genet 1979 Oct 01
PMID:A novel priming system for conjugal synthesis of an IncI alpha plasmid in recipients. 39 29
A cold-sensitive mutation in the rpoB gene for the
RNA polymerase
beta subunit increasing the temperature of promoter opening on T2 phage DNA was obtained in Escherichia coli. The mutation also affects the stages preceding promoter opening by increasing the dissociation rate of
RNA polymerase
--DNA closed complexes. The affinity of
RNA polymerase
to T2 and lambda DNA is differentially changed by the mutation. The relative efficiency of transcription of these two templates is also changed. These results suggest a participation of the
RNA polymerase
beta subunit in the interaction with promoters.
Mol
Gen
Genet 1979 Oct 02
PMID:A cold-sensitive beta subunit mutant RNA polymerase from Escherichia coli with defects in promoter opening in vitro. 39 44
The molecular structure of RNA polymerases from Escherichia coli, Salmonella typhimurium, Salmonella anatum,serratia marcescens, Aerobacter aerogens, Proteus mirabilis and Bacillus subtilis were compared based on:i) inhibition of the enzyme activity by treatment with antibodies against E. coli
RNA polymerase
subunits;ii) analysis of antibody precipitates by sodium ododecyl sulfatepolyacrylamide gel electrophoresis; and iii) analysis of antibody precipitates by urea-isoelectrofocusing followed by sodium dodecyl sulfate-slab gel electrophoresis in the second dimension. All the bacterial RNA polymerases examined cross-react equally with anti-E. COLI HOLOPOLYMERASE BUT EXHIbit different extents of cross-reaction with antibodies against individual subunits. Except for B. subtilis
RNA polymerase
, the molecular weight and isoelectric point of the enzyme subunits are close to those of E. coli polymerase. However, minor difference were found at least within the resolution of the techniques employed:S. anatum polymerase has sigma subunit larger than E. coli sigma subunit; P. mirabilis enzyme has sigma subunit larger in size and more acidic in charge, and alpha subunit smaller and more basic than corresponding E. coli subunits. The electrophoretic map of B. subtilis enzyme subunits is completely different from that of E. coli enzyme.
Mol
Gen
Genet 1977 Jul 20
PMID:Comparative studies of RNA polymerase subunits from various bacteria. 40
Recombinants of human influenza type A viruses, A/Krasnodar/101/1959 (H2N2) or A/Habarovsk/15/1976 (H3N2), and fowl plague virus (FPV), strain Weybridge (Hav1Neq1) were obtained. The genome of the recombinant obtained by recombination of influenza A/Habarovsk/15/1976 virus and FPV contained the genes 4 (HA) and 6 (NA) derived from the influenza A/Habarovsk virus and all the other genes [1, 2, 3, 5 (NP), 7 (M), 8 (NS)] from FPV. The genome of the recombinant of A/Krasnodar/101/1959 virus and FPV contained the genes 2, 4 (HA) and 6 (NA) derived from influenza A/Krasnodar virus and all the other genes [1, 3, 5, (NP), 7 (M), 8 (NS)] from FPV. The recombinants, like FPV, gave high virus yields in chick embryos and could multiply at high temperatures (40 and 42 degrees C), but, like human influenza viruses, were non-pathogenic for chickens and did not replicate in chick embryo fibroblast culture, but did replicate in a human conjunctiva cell line, clone 1-5C-4. The virion
transcriptase
of the recombinants, in a number of properties determined in vitro, was similar to FPV
transcriptase
but not to the human influenza virus enzyme.
J
Gen
Virol 1979 Apr
PMID:Investigation of recombinants of human influenza and fowl plague viruses. 47 41
RNA 1 (see end of Summary) of a cold-adapted and temperature-sensitive (ts) influenza virus mutant A/Ann Arbor/6/60 has a different mobility from RNA 1 of wild-type (wt) A/Ann Arbor/6/60 when subjected to electrophoresis through acrylamide/agarose gels in the absence of denaturing agents. Detection of this lesion in RNA 1 of the mutant virus was dependent on the temperature of the gel during electrophoresis. Because RNA 1 is believed to code for a protein involved in virus-specific RNA synthesis we compared phenotypes of virion transcriptases in the wt and mutant viruses. The enzyme of the mutant virus was found to be about 40% less active at 40 degrees C than the enzyme of the wt virus when related to their activities at 31 degrees C. Two cold-adapted ts recombinants which derive their RNA 1 from the mutant A/Ann Arbor/6/60 have virion transcriptases with a phenotype similar to that of their mutant parent. Three different cold-adapted ts recombinants, however, which also derive their RNA 1 from the mutant A/Ann Arbor/6/60, have virion transcriptases with a phenotype similar to that of wt virus. We conclude, therefore, that the conditional-lethal ts property of A/Ann Arbor/6/60 mutant and its recombinants is independent of the phenotypic marker observed for the A/Ann Arbor/6/60 mutant virion
transcriptase
, and that the lesion in RNA 1 of the mutant may also be unrelated to the observed difference between virion transcriptases of the mutant and wt A/Ann Arbor/6/60 viruses. The phenotypes of the virion transcriptases in recombinants did, however, correlate with the derivation of their RNA 2. This suggests that the increased temperature-sensitivity of virion
transcriptase
of the A/Ann Arbor/6/60 mutant is caused by either (1) a lesion (not necessarily conditionally lethal) that occurred in its RNA 2 during the course of cold-adaptation, or (2) a lesion in another gene whose product is a component of the virion
transcriptase
complex, but which lesion is only expressed phenotypically when there is a synergistic interaction in the
transcriptase
complex with the product of A/Ann Arbor/6/60 rna 2.
J
Gen
Virol 1979 Aug
PMID:Comparative studies of wild-type and cold-mutant (temperature-sensitive) influenza viruses: independent segregation of temperature-sensitivity of virus replication from temperature-sensitivity of virion transcriptase activity during recombination of mutant A/Ann Arbor/6/60 with wild-type H3N2 strains. 52 98
We have demonstrated by recombination of two highly pathogenic avian influenza viruses [A/FPV/Rostock (Hav1N1) x A/turkey/England/63 (Hav1Nav3)] that recombinants can be isolated which are pathogenic as well as non-pathogenic for chickens. They carried the glycoproteins of either parent strains, and all are produced in infectious form in chick embryo cells. Genetic analysis revealed that the non-pathogenic recombinants possess a mixed
RNA polymerase
complex, consisting of pol 1, pol 2, ptra and NP gene products, while, with one exception, the pathogenic recombinants have the genes coding for the polymerase activity from one or other parent virus. The biological properties of the recombinant viruses did not correlate with their pathogenicity for chickens.
J
Gen
Virol 1979 Aug
PMID:Correlation of pathogenicity and gene constellation of influenza A viruses. III. Non-pathogenic recombinants derived from highly pathogenic parent strains. 52 99
Human coronavirus RNA, prepared by extraction of purified virions with phenol-chloroform, consists of a major 15 to 55S class and a minor 4S class of RNA fragments. Polyadenylic acid [poly (A)] sequences are present in 15 to 55S but not in 4S RNA, suggesting different functions for each class. A stretch of poly (A) of approximately 19 adenosine monophosphate residues was obtained in sizing experiments after digesting OC-43 RNA with pancreatic and T1 ribonucleases. An OC-43 virion
RNA transcriptase
could not be detected with systems optimal for detecting the transcriptases of influenza and Newcastle disease virus.
J
Gen
Virol 1978 Apr
PMID:Presence of genomic polyadenylate and absence of detectable virion transcriptase in human coronavirus OC-43. 64 31
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