Effect of a brain-specific protein (S-100 protein) on the nucleolar RNA polymerase activity in isolated brain nuclei

1973 ◽  
Vol 29 (12) ◽  
pp. 1499-1501 ◽  
Author(s):  
N. Miani ◽  
F. Michetti ◽  
G. de Renzis ◽  
A. Caniglia
Keyword(s):  
Rna Polymerase ◽  
Protein S ◽  
Polymerase Activity ◽  
Specific Protein ◽  
Brain Nuclei ◽  
S 100 ◽  
Rna Polymerase Activity ◽  
Nucleolar Rna

scholarly journals The action of α-amanitin in vivo on the synthesis and maturation of mouse liver ribonucleic acids

1974 ◽  
Vol 138 (3) ◽  
pp. 321-333 ◽  
Author(s):  
Asen A. Hadjiolov ◽  
Mariana D. Dabeva ◽  
Vladimir V. Mackedonski
Keyword(s):  
Rna Polymerase ◽  
Polymerase Activity ◽  
5S Rrna ◽  
Gene Products ◽  
Ribonucleic Acids ◽  
Rrna Maturation ◽  
Rna Polymerase Activity ◽  
Nucleolar Rna

α-Amanitin acts in vitro and in vivo as a selective inhibitor of nucleoplasmic RNA polymerases. Treatment of mice with low doses of α-amanitin causes the following changes in the synthesis, maturation and nucleocytoplasmic transfer of liver RNA species. 1. The synthesis of the nuclear precursor of mRNA is strongly inhibited and all electrophoretic components are randomly affected. The labelling of cytoplasmic mRNA is blocked. These effects may be correlated with the rapid and lasting inhibition of nucleoplasmic RNA polymerase. 2. The synthesis and maturation of the nuclear precursor of rRNA is inhibited within 30min. (a) The initial effect is a strong (about 80%) inhibition of the early steps of 45S precursor rRNA maturation. (b) The synthesis of 45S precursor rRNA is also inhibited and the effect increases from about 30% at 30min to more than 70% at 150min. (c) The labelling of nuclear and cytoplasmic 28S and 18S rRNA is almost completely blocked. The labelling of nuclear 5S rRNA is inhibited by about 50%, but that of cytoplasmic 5S rRNA is blocked. (d) The action of α-amanitin on the synthesis of precursor rRNA cannot be correlated with the slight gradual decrease of nucleolar RNA polymerase activity (only 10–20% inhibition at 150min). (e) The inhibition of precursor rRNA maturation and synthesis precedes the ultrastructural lesions of the nucleolus detected by standard electron microscopy. 3. The synthesis of nuclear 4.6S precursor of tRNA is not affected by α-amanitin. However, the labelling of nuclear and cytoplasmic tRNA is decreased by about 50%, which indicates an inhibition of precursor tRNA maturation. The results of this study suggest that the synthesis and maturation of the precursor of rRNA and the maturation of the precursor of tRNA are under the control of nucleoplasmic gene products. The regulator molecules may be either RNA or proteins with exceedingly fast turnover.

Studies on Isolated Brain Nuclear DNA-Dependent RNA Polymerase

1972 ◽  
Vol 50 (3) ◽  
pp. 299-304 ◽  
Author(s):  
Vijendra K. Singh ◽  
S. C. Sung
Keyword(s):  
Enzyme Activity ◽  
Rna Polymerase ◽  
Actinomycin D ◽  
Nuclear Dna ◽  
Divalent Cations ◽  
Polymerase Activity ◽  
Maximum Activity ◽  
Optimum Concentration ◽  
Brain Nuclei ◽  
Rna Polymerase Activity

DNA-dependent RNA polymerase, which was isolated from beef brain nuclei, was stimulated by Mn2+ and Mg2+. The polymerase was about four times as active with Mn2+ as with Mg2+ but both of these divalent cations were required for maximum activity. KCl stimulated the enzyme activity with an optimum concentration around 0.2 M. The stimulation by KCl was much more pronounced in the presence of Mn2+ or Mn2+ plus Mg24 than in the presence of Mg2+ alone. Spermidine and spermine also stimulated the RNA polymerase activity and this stimulation was much greater in the presence of Mn2+ than in the presence of Mg2+ or both together. With Mn2+ plus Mg2+, spermidine had little or no stimulatory effect when heat-denatured DNA served as template, whereas with Mn2+ alone, spermidine markedly stimulated the enzyme in the presence of either native or heat-denatured DNA. The effect of spermidine was different with Mg2+ alone. The enzyme was inhibited as much as 75% by actinomycin D and almost completely by α-amanitin but not by rifampicin. Yeast RNA inhibited the enzyme activity considerably while spermidine appeared to overcome and prevent this inhibition of RNA polymerase.

scholarly journals Cortisone Stimulation of Nucleolar RNA Polymerase Activity

1971 ◽  
Vol 68 (9) ◽  
pp. 2177-2180 ◽  
Author(s):  
F.-L. Yu ◽  
P. Feigelson
Keyword(s):  
Rna Polymerase ◽  
Polymerase Activity ◽  
Rna Polymerase Activity ◽  
Nucleolar Rna ◽  
Stimulation Of

Effect of the S-100 protein on the RNA-polymerase activity in brain nucleoli isolated from newborn rat

1976 ◽  
Vol 2 (1) ◽  
pp. 23-27 ◽  
Author(s):  
Fabrizio Michetti ◽  
Gabriella DeRenzis
Keyword(s):  
Rna Polymerase ◽  
Polymerase Activity ◽  
Newborn Rat ◽  
S 100 ◽  
Rna Polymerase Activity

Brain-specific effect of the S-100 protein on the RNA-polymerase / activity in isolated nuclei

1976 ◽  
Vol 105 (2) ◽  
pp. 372-375 ◽  
Author(s):  
Fabrizio Michetti ◽  
Gabriella De Renzis ◽  
Rosario Donato ◽  
Nicolo` Miani
Keyword(s):  
Rna Polymerase ◽  
Specific Effect ◽  
Polymerase Activity ◽  
Isolated Nuclei ◽  
S 100 ◽  
Rna Polymerase Activity

AN ASSAY FOR RNA POLYMERASE ACTIVITY IN RAT BRAIN NUCLEI: EFFECTS OF INJECTION OF OESTRADIOL BENZOATE

1980 ◽  
Vol 85 (2) ◽  
pp. 341-347 ◽  
Author(s):  
B. D. GREENSTEIN
Keyword(s):  
Rna Polymerase ◽  
Rat Brain ◽  
Preliminary Evidence ◽  
Polymerase Activity ◽  
Female Rats ◽  
Oestrogen Receptors ◽  
Guanosine Triphosphate ◽  
Brain Nuclei ◽  
Oestradiol Benzoate ◽  
Rna Polymerase Activity

A sensitive, reliable assay of activity of RNA polymerase in purified nuclei from the rat brain is described. The assay measured the incorporation of [3H]guanosine triphosphate into RNA by nuclei. Little incorporation occurred in the presence of α-amanitin (400 ng) suggesting that RNA polymerase B activity was being measured. Preliminary evidence showed that after administration of oestradiol benzoate to 18-day-old female rats RNA polymerase activity was raised in areas of brain known to contain oestrogen receptors.

Changes in RNA polymerase activity in isolated mouse uterine nuclei during the decidual cell reaction

1978 ◽  
Vol 521 (1) ◽  
pp. 267-273 ◽  
Author(s):  
M.J. Serra ◽  
B.E. Ledford ◽  
J.C. Rankin ◽  
B. Baggett
Keyword(s):  
Rna Polymerase ◽  
Polymerase Activity ◽  
Decidual Cell ◽  
Cell Reaction ◽  
Rna Polymerase Activity

Functional analysis of influenza rna polymerase activity by the use of caps, oligonucleotides and polynucleotides

1981 ◽  
Vol 1 (2) ◽  
pp. 97-105 ◽  
Author(s):  
S. Stridh ◽  
B. Öberg ◽  
J. Chattopadhyaya ◽  
S. Josephson
Keyword(s):  
Functional Analysis ◽  
Rna Polymerase ◽  
Polymerase Activity ◽  
Rna Polymerase Activity

Pharmaceutical interference of the EWS-FLI1-driven transcriptome by co-targeting H3K27ac and RNA polymerase activity in Ewing Sarcoma

2021 ◽  
pp. molcanther.MCT-20-0489-A.2020
Author(s):  
Daniel A. R. Heisey ◽  
Sheeba Jacob ◽  
Timonthy L Lochmann ◽  
Richard Kurupi ◽  
Maninderjit S. Ghotra ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Ewing Sarcoma ◽  
Polymerase Activity ◽  
Rna Polymerase Activity

RNA polymerase activity in virions from Ustilago maydis

1984 ◽  
Vol 4 (1) ◽  
pp. 188-194
Author(s):  
B S Ben-Tzvi ◽  
Y Koltin ◽  
M Mevarech ◽  
A Tamarkin
Keyword(s):  
Rna Polymerase ◽  
Viral Genome ◽  
Ustilago Maydis ◽  
Polymerase Activity ◽  
Reaction Products ◽  
Double Stranded Rna ◽  
Rna Molecules ◽  
Rna Transcripts ◽  
Rna Polymerase Activity

RNA polymerase activity is associated with the double-stranded RNA virions of Ustilago maydis. The reaction products of the polymerase activity are single-stranded RNA molecules. The RNA molecules synthesized are homologous to the three classes of double-stranded RNA molecules that typify the viral genome. The single-stranded RNA synthesized is released from the virions. The molecular weight of the single-stranded RNA transcripts is about half the size of the double-stranded RNA segments, and thus, it appears that in the in vitro reaction, full-length transcripts can be obtained.

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