Transcription of rat liver chromatin and DNA by homologous and E. coli RNA polymerase

1974 ◽  
Vol 3 (1) ◽  
pp. 27-33 ◽  
Author(s):  
Maurice Dupras ◽  
James Bonner
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
E Coli ◽  
Liver Chromatin

scholarly journals Two species of RNA polymerase II released from rat liver chromatin

FEBS Letters ◽  
1979 ◽  
Vol 104 (1) ◽  
pp. 169-172 ◽  
Author(s):  
Munehiko Yukioka ◽  
Koichiro Omori ◽  
Yasuji Okai ◽  
Akira Inoue
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rat Liver ◽  
Liver Chromatin

scholarly journals Location of endogenous RNA polymerase B in a sub-fraction of rat liver chromatin

FEBS Letters ◽  
1976 ◽  
Vol 61 (2) ◽  
pp. 166-170 ◽  
Author(s):  
Etienne Pays ◽  
Jacqueline Flamand
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
Liver Chromatin

Evidence for the transcription of physiologically inactive rat-liver nucleolar chromatin by Escherichia coli RNA polymerase

1982 ◽  
Vol 2 (3) ◽  
pp. 155-161 ◽  
Author(s):  
Fu-Li Yu ◽  
Annabella Barrett
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Rat Liver ◽  
Dnase I ◽  
Rna Polymerase I ◽  
E Coli ◽  
Chromatin Template ◽  
Nucleolar Chromatin ◽  
Polymerase I ◽  
Active Genes

Rat-liver nucleoli (10–15 pg DNA) were digested with either 0.6 or 3 units of DNase I for various times (up to 1 h). RNA synthesis was then measured in the absence or presence ol 3 units of Escherichia coli RNA polymerase. It was found that the nucleolar chromatin supporting the endogenous engaged RNA polymerase I transcription was compl-etely destroyed in 3 min with either concentration of DNase I. The nucleolar chromatin template transcribed by E. coli RNA polymerase retained 50% of its original capacity even 60 min alter 3 units of DNase I digestion. When hybridization experiments were conducted, it was found that the DNAs derived from both levels of DNase-Idigested nucleoli were incapable of forming hybrids with the labelled nucleolar RNA synthesized by the engaged RNA polymerase I from the untreated nucleoli. Since the engaged RNA polymerase I transcribes only the physiologically active genes of the nucleolar chromatin, and the RNA transcripts represent active gene product, these data suggest that DNase I digestion has completely destroyed the active genes of the nucleolar chromatin, and E. coli RNA polymerase is able to transcribe the inactive nucleolar chromatin template.

scholarly journals Characterization of double-stranded ribonucleic acid sequences present in the initial transcription products of rat liver chromatin

1977 ◽  
Vol 165 (2) ◽  
pp. 237-245 ◽  
Author(s):  
E Pays
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Rat Liver ◽  
Rna Sequences ◽  
Complementary Sequences ◽  
Exogenous Rna ◽  
Liver Chromatin ◽  
Low Ionic Strength

At low ionic strength and with a low exogenous RNA polymerase/DNA ratio, rat liver chromatin directs the synthesis in vitro of RNA sequences rich in double-stranded segments. All the transcripts contain at least one double-stranded sequence. Most of the double-stranded segments are formed by intramolecular base-pairing of inverted complementary sequences separated by a single-stranded loop. They are heterogeneous in size, 35-45% of them being more than 80 nucleotides long. They contain 61-64% G+C, whether synthesized by rat liver RNA polymerase (form B) or Escherichia coli RNA polymerase. The largest double-stranded sequences are found in the largest transcripts, and are the most thermostable. The fidelity of base-matching is better in double-stranded transcripts synthesized on rat liver chromatin by homologous polymerase than in those synthesized on it by a bacterial polymerase, or in those synthesized by either of the two polymerases on pure DNA.

Transcription of chemically acetylated chromatin with homologous RNA polymerase B

1984 ◽  
Vol 4 (2) ◽  
pp. 155-163 ◽  
Author(s):  
A. Csordas ◽  
I. Multhaup ◽  
H. Grunicke
Keyword(s):  
Acetic Anhydride ◽  
Rna Polymerase ◽  
Rat Liver ◽  
Fold Increase ◽  
New Method ◽  
Liver Chromatin ◽  
High Degree

Homologous RNA polymerase B was used to examine the template properties of rat liver chromatin modified by acetic anhydride. Transcription of chromatin was strongly stimulated on the chemically acetyiated template. Under conditions of reinitiation inhibition there was an approximately two-fold increase in the number of initiation sites on the acetylated chromatin. A new method of chemical acetylation of histones, with a high degree of specificity, is presented.

α Amanitin, a specific inhibitor of transcription by mammalian RNA-polymerase

1969 ◽  
Vol 24 (12) ◽  
pp. 1538-1544 ◽  
Author(s):  
K. H. Seifart ◽  
C. E. Sekeris
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
Potent Inhibitor ◽  
Specific Inhibitor ◽  
Amanita Phalloides ◽  
Chain Initiation ◽  
E Coli ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Mammalian Enzyme

Evidence has been presented that α amanitin. the potent bicyclic polypeptide toxin of the toadstool amanita phalloides inhibits transcription by purified RNA polymerase from rat liver nuclei. This inhibition is highly specific for the mammalian enzyme, since it does not impede the same reaction catalyzed by the enzyme from E. coli thus rendering an interaction between the template and inhibitor very unlikely. α Amantitin is a very potent inhibitor and calculations show an approximate stoichiometry of 1 : 1 between enzyme and inhibitor. In addition, evidence is formarded suggesting that the inhibitor allows chain initiation to occur, but abruptly inhibits elongation of RNA chains.

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