scholarly journals Influence of irofulven, a transcription-coupled repair-specific antitumor agent, on RNA polymerase activity, stability and dynamics in living mammalian cells

2008 ◽  
Vol 121 (8) ◽  
pp. 1275-1283 ◽  
Author(s):  
A. E. Escargueil ◽  
V. Poindessous ◽  
D. G. Soares ◽  
A. Sarasin ◽  
P. R. Cook ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Mammalian Cells ◽  
Antitumor Agent ◽  
Polymerase Activity ◽  
Rna Polymerase Activity ◽  
Transcription Coupled Repair

scholarly journals Transcription of brain chromatin by ribonucleic acid polymerases from brain nucleic and from Escherichia coli

1972 ◽  
Vol 130 (4) ◽  
pp. 1095-1099 ◽  
Author(s):  
Vijendra K. Singh ◽  
S. C. Sung
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Mammalian Cells ◽  
Transcriptional Control ◽  
Polymerase Activity ◽  
Control Mechanisms ◽  
E Coli ◽  
Bacterial Enzyme ◽  
Rna Polymerase Activity

1. Transcription of ox brain chromatin by brain nuclear RNA polymerase II and Escherichia coli RNA polymerase was studied. 2. The soluble chromatin prepared from brain nuclei contained DNA, RNA, histone and non-histone proteins. Such chromatin preparations did not display any endogenous RNA polymerase activity, when assayed in the presence of concentrations of KCl as high as 0.4m. 3. The chromatin-templated activity of brain nuclear polymerase II was stimulated by KCl, with an optimum around 0.25m. 4. The template activity of brain chromatin for brain nuclear polymerase II and E. coli enzyme was about 20–25% of that of pure DNA. This greatly repressed templatecapacity of chromatin was probably due to the acid-soluble chromosomal proteins. 5. Brain nuclear polymerase II was 3–4 times more active with dehistonized chromatin than with pure DNA as template, whereas bacterial enzyme was almost equally active with either of these two templates, reflecting the specificity of the transcriptional control mechanisms in mammalian cells.

scholarly journals NAD+, ADP-ribosylation and transcription in permeabilized mammalian cells

1981 ◽  
Vol 199 (3) ◽  
pp. 813-817 ◽  
Author(s):  
J Walker ◽  
C K Pearson
Keyword(s):  
Rna Polymerase ◽  
Mammalian Cells ◽  
Inhibitory Effect ◽  
Polymerase Activity ◽  
Rna Polymerase I ◽  
Permeabilized Cells ◽  
Adp Ribosylation ◽  
Deoxyribonuclease I ◽  
Rna Polymerase Activity ◽  
Polymerase I

When permeabilized hamster fibroblasts were incubated with 4 mM-NAD+, the substrate for poly(ADP-ribose) polymerase, RNA polymerase I activity was inhibited by about 85%. This inhibition was not relieved by prior incubation of cells with 3-aminobenzamide, a potent inhibitor of the poly(ADP-ribose) polymerase. Digestion of cells with pancreatic deoxyribonuclease I resulted in the inhibition of RNA polymerase I by 80% and the activation of poly(ADP-ribose) polymerase by up to 300%; prior incubation with 3-aminobenzamide did not prevent the inhibition of the RNA polymerase activity. No radioactivity was found associated with RNA polymerase I during later stages of purification of this enzyme from permeabilized cells previously incubated with [14C]NAD+. The inhibitory effect of NAD+ on RNA polymerase I was not specific for NAD+, as other small, negatively charged molecules with a nuclear location also inhibited the enzyme. The results do not support the concept of a role for ADP-ribosylation in transcription catalysed by RNA polymerase I.

A Possible Role of Lipids in RNA Polymerase from Mammalian Cells

1972 ◽  
Vol 50 (7) ◽  
pp. 807-812 ◽  
Author(s):  
I. A. Menon
Keyword(s):  
Rna Polymerase ◽  
Phospholipase D ◽  
Mammalian Cells ◽  
Polymerase Activity ◽  
Ionic Concentration ◽  
Phospholipase A ◽  
Rat Tissues ◽  
Rna Polymerase Activity ◽  
Liver Nuclei

The effects of treatment with phospholipases and extraction with solvents on the activities of RNA polymerases from several rat tissues were studied. The RNA polymerase activity of particulate enzyme from rat liver nuclei was decreased by pretreatment of the enzyme with phospholipase A. The phospholipase decreased the RNA polymerase activity in presence of Mg2+ but not that in presence of Mn2+. The effect of phospholipase A was observed only at low ionic concentration. When the RNA polymerase activity was determined in presence of ammonium sulfate, KCl, or NaCl, phospholipase A did not decrease the RNA polymerase activity. Extraction of the RNA polymerase with ether or iso-octane decreased the RNA polymerase activity to approximately the same extent as the pretreatment with phospholipase A. Phospholipase C produced similar changes as phospholipase A but phospholipase D and lipase did not have any effect on the RNA polymerase activity. Treatment with phospholipase A as well as extraction with solvents enhanced the activity of chromatin-bound RNA polymerase from rat brain, and the RNA polymerase activities of similar preparations from spleen, kidney, heart, and lung were affected only to a relatively smaller extent.

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.

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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