scholarly journals Modification of the template capacity of liver chromatin for form-B ribonucleic acid polymerase by food intake in rats under controlled feeding schedules

1975 ◽  
Vol 146 (3) ◽  
pp. 687-696 ◽  
Author(s):  
B Barbiroli ◽  
B Tadolini ◽  
M S Moruzzi ◽  
M G Monti
Keyword(s):  
Ionic Strength ◽  
Food Intake ◽  
Rna Polymerase ◽  
Dark Period ◽  
Polymerase Activity ◽  
Nuclear Chromatin ◽  
Feeding Period ◽  
Period 2 ◽  
Liver Chromatin ◽  
Rna Polymerase Activity

Nuclei from liver of rats accustomed to eating during the first 8h of a daily 12h dark period demonstrate an increased capacity to synthesize RNA 6H after the beginning of the feeding period. 2. This increase is accompanied by a higher yield of extractable form-B DNA-dependent RNA polymerase activity. 3. The endogenous RNA polymerase activity associated with nuclear chromatin is also stimulated by food intake. Both purified and chromatin-associated form-B enzyme activities exhibit different ionic strength requirements after food intake. 4. The sensitivity of exogenous (added) form-B-enzyme to changes in ionic strength changes after feeding when chromatin is used as template. 5. Chromatin extracted from the liver of fed rats is a better template for form-B-enzyme than chromatin extracted from starved rats.

More evidence for replication-transcription-coupling in Physarum polycephalum

1980 ◽  
Vol 41 (1) ◽  
pp. 105-113
Author(s):  
G. Pierron ◽  
H.W. Sauer
Keyword(s):  
Ionic Strength ◽  
Rna Polymerase ◽  
Physarum Polycephalum ◽  
Mitotic Cycle ◽  
Polymerase Activity ◽  
S Phase ◽  
Isolated Nuclei ◽  
Rna Polymerase Activity ◽  
High Level ◽  
Alpha Amanitin

Endogenous RNA polymerase activity of isolated nuclei from Physarum polycephalum was determined at high (400 mM KCl) and low (5–100 mM KCl) ionic strength. The activity of RNA polymerase B (alpha-amanitin-sensitive UMP incorporation) and of RNA polymerase A (plus C) (alpha-amanitin-resistant UMP incorporation) was compared in accurately sized nuclear samples derived from macroplasmodia at distinct points of the mitotic cycle. Minimum total RNA polymerase activity was detected in metaphase nuclei. A constant level of RNA polymerase B activity was detected at all other stages of the mitotic cycle, if nuclei were assayed at high ionic strength. However, a high level in S-phase, a low level in G2-phase and again a high level in early prophase were measured, if nuclei were assayed at low ionic strength. Inhibition of DNA synthesis by hydroxyurea in vivo had a selective and drastic effect on in vitro RNA polymerase activity of isolated nuclei derived from S-phase plasmodia, yielding up to 100% inhibition in early S-phase.

Chromosomale Strukturen von Pseudomonas testosteroni. II. Aktivität der endogenen RNA-Polymerase /Chromosomal Structure of Pseudomonas testosteroni. II. Activity of the Endogenous RNA-Polymerase

1976 ◽  
Vol 31 (9-10) ◽  
pp. 601-605 ◽  
Author(s):  
Günter Reimer ◽  
Dusan Drahovsky
Keyword(s):  
Ionic Strength ◽  
Rna Polymerase ◽  
Protein Complexes ◽  
Polymerase Activity ◽  
Chromosomal Dna ◽  
Chromosomal Structure ◽  
Dna Structures ◽  
Rna Polymerase Activity ◽  
Pseudomonas Testosteroni

Abstract After careful lysis the nucleoid of Pseudomonas testosteroni can be isolated in three different forms with compact and unfolded DNA structures 1. The released nucleoids contain endogenous DNA-dependent RNA-polymerase activity using the chromosomal DNA as a template. RNA syn­ thesis is proportional to duration of RNA-polymerase reaction and amount of DNA-protein-complexes. The sensitivity towards ionic strength and rifampicin indicates that a part of RNA-polymerase activity is tightly bound to the chromosomal DNA.

scholarly journals Differential inhibition of mammalian ribonucleic acid polymerases by an exotoxin from Bacillus thuringiensis. The direct observation of nucleoplasmic ribonucleic acid polymerase activity in intact nuclei

1972 ◽  
Vol 127 (4) ◽  
pp. 619-624 ◽  
Author(s):  
T. Beebee ◽  
A. Korner ◽  
R. P. M. Bond
Keyword(s):  
Ionic Strength ◽  
Bacillus Thuringiensis ◽  
Rna Polymerase ◽  
Ribonucleic Acid ◽  
Polymerase Activity ◽  
High Ionic Strength ◽  
Rna Polymerases ◽  
Differential Inhibition ◽  
Rna Polymerase Activity ◽  
Soluble Enzymes

The effects of the exotoxin from Bacillus thuringiensis on DNA-dependent RNA polymerases from rat liver were examined. The exotoxin inhibits all RNA polymerase activity at both low and high ionic strength in intact nuclei, and soluble enzymes are similarly affected. This inhibition is relieved by ATP. Dephosphorylated exotoxin did not inhibit the soluble enzymes. Nucleolar and nucleoplasmic RNA polymerases respond to different concentration ranges of exotoxin, and the compound can be used in intact nuclei to isolate the nucleoplasmic activity.

scholarly journals Effect of Phenylhydrazine-induced Hemolytic Anemia on Nuclear RNA Polymerase Activity of the Mouse Spleen

Blood ◽  
1973 ◽  
Vol 42 (2) ◽  
pp. 257-266 ◽  
Author(s):  
Jerry L. Spivak ◽  
Dennis Toretti ◽  
Herbert W. Dickerman
Keyword(s):  
Ionic Strength ◽  
Rna Polymerase ◽  
Hemolytic Anemia ◽  
Nuclear Dna ◽  
Polymerase Activity ◽  
Tenfold Increase ◽  
Rna Polymerase Activity ◽  
Low Ionic Strength ◽  
Dna Template ◽  
Nuclear Rna Polymerase

Abstract The DNA-dependent RNA polymerase of nuclei from lymphoid-rich and erythroid-rich mouse spleens was compared in regard to requirements and conditions of the reactions. The inhibition by either actinomycin D or pancreatic DNase indicated that a DNA template was required for the observed reactions. Following the induction of a hemolytic anemia by the administration of phenylhydrazine, there was a tenfold increase in the nuclear polymerase activity per milligram nuclear DNA of the developing erythropoietic spleen when the assays were done at low ionic strength and more than a threefold increase at high ionic strength. The peak rise in polymerase activity precedes the maximal development of the erythropoietic spleen by 3 days.

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.

scholarly journals HDAC6 Restricts Influenza A Virus by Deacetylation of the RNA Polymerase PA Subunit

2018 ◽  
Vol 93 (4) ◽  
Author(s):  
Huan Chen ◽  
Yingjuan Qian ◽  
Xin Chen ◽  
Zhiyang Ruan ◽  
Yuetian Ye ◽  
...  
Keyword(s):  
Life Cycle ◽  
Rna Polymerase ◽  
Influenza A Virus ◽  
Influenza A ◽  
Molecular Mechanisms ◽  
Polymerase Activity ◽  
Negative Regulator ◽  
Host Protein ◽  
Spectrometric Analysis ◽  
Rna Polymerase Activity

ABSTRACT The life cycle of influenza A virus (IAV) is modulated by various cellular host factors. Although previous studies indicated that IAV infection is controlled by HDAC6, the deacetylase involved in the regulation of PA remained unknown. Here, we demonstrate that HDAC6 acts as a negative regulator of IAV infection by destabilizing PA. HDAC6 binds to and deacetylates PA, thereby promoting the proteasomal degradation of PA. Based on mass spectrometric analysis, Lys(664) of PA can be deacetylated by HDAC6, and the residue is crucial for PA protein stability. The deacetylase activity of HDAC6 is required for anti-IAV activity, because IAV infection was enhanced due to elevated IAV RNA polymerase activity upon HDAC6 depletion and an HDAC6 deacetylase dead mutant (HDAC6-DM; H216A, H611A). Finally, we also demonstrate that overexpression of HDAC6 suppresses IAV RNA polymerase activity, but HDAC6-DM does not. Taken together, our findings provide initial evidence that HDAC6 plays a negative role in IAV RNA polymerase activity by deacetylating PA and thus restricts IAV RNA transcription and replication. IMPORTANCE Influenza A virus (IAV) continues to threaten global public health due to drug resistance and the emergence of frequently mutated strains. Thus, it is critical to find new strategies to control IAV infection. Here, we discover one host protein, HDAC6, that can inhibit viral RNA polymerase activity by deacetylating PA and thus suppresses virus RNA replication and transcription. Previously, it was reported that IAV can utilize the HDAC6-dependent aggresome formation mechanism to promote virus uncoating, but HDAC6-mediated deacetylation of α-tubulin inhibits viral protein trafficking at late stages of the virus life cycle. These findings together will contribute to a better understanding of the role of HDAC6 in regulating IAV infection. Understanding the molecular mechanisms of HDAC6 at various periods of viral infection may illuminate novel strategies for developing antiviral drugs.

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