Degree of inhibition of eukaryotic DNA-dependent RNA polymerases by thuringiensin

1981 ◽  
Vol 46 (3) ◽  
pp. 673-677
Author(s):  
Květa Horská ◽  
Karel Šebesta
Keyword(s):  
Rna Polymerases ◽  
Calf Thymus ◽  
Eukaryotic Dna

It was shown in experiments with purified DNA-dependent RNA polymerases from calf thymus that the inhibition of these enzymes caused by thuringiensin is competitive with respect to ATP. Enzyme AI is more sensitive to the inhibitor (Ki = 0.34 μm) than enzyme B (Ki = 1.49 μm).This finding eliminates the discrepancies with respect to this subject which exist in literature.

Early evolution of eukaryotic DNA-dependent RNA polymerases

2008 ◽  
Vol 24 (5) ◽  
pp. 211-215 ◽  
Author(s):  
Marta Kwapisz ◽  
Frédéric Beckouët ◽  
Pierre Thuriaux
Keyword(s):  
Rna Polymerases ◽  
Early Evolution ◽  
Eukaryotic Dna

Calf thymus RNA polymerases exhibit template specificity

1970 ◽  
Vol 38 (6) ◽  
pp. 1033-1040 ◽  
Author(s):  
M. Gniazdowski ◽  
J.L. Mandel ◽  
F. Gissinger ◽  
C. Kedinger ◽  
P. Chambon
Keyword(s):  
Rna Polymerases ◽  
Calf Thymus ◽  
Template Specificity

Chapter 1. Isolation and Assay of Eukaryotic DNA-Dependent RNA Polymerases

1978 ◽  
pp. 1-26 ◽  
Author(s):  
Pablo Valenzuela ◽  
Graeme I. Bell ◽  
Fanyela Weinberg ◽  
William J. Rutter
Keyword(s):  
Rna Polymerases ◽  
Eukaryotic Dna

Effect of polyribonucleotides on eukaryotic DNA-dependent RNA polymerases

1974 ◽  
Vol 366 (4) ◽  
pp. 435-442 ◽  
Author(s):  
Ryuzo Sasaki ◽  
Hideyuki Goto ◽  
Kenji Arima ◽  
Yukiko Sasaki
Keyword(s):  
Rna Polymerases ◽  
Eukaryotic Dna

scholarly journals Animal DNA-Dependent RNA Polymerases. 1. Large-Scale Solubilization and Separation of A and B Calf-Thymus RNA-Polymerase Activities

1972 ◽  
Vol 28 (2) ◽  
pp. 269-276 ◽  
Author(s):  
Claude Kedinger ◽  
Francis Gissinger ◽  
Marek Gniazdowski ◽  
Jean-Louis Mandel ◽  
Pierre Chambon
Keyword(s):  
Rna Polymerase ◽  
Large Scale ◽  
Rna Polymerases ◽  
Calf Thymus

scholarly journals Functional Characterization of ABC10α, an Essential Polypeptide Shared by All Three Forms of Eukaryotic DNA-dependent RNA Polymerases

1999 ◽  
Vol 274 (44) ◽  
pp. 31485-31492 ◽  
Author(s):  
Liudmilla Rubbi ◽  
Sylvie Labarre-Mariotte ◽  
Stéphane Chédin ◽  
Pierre Thuriaux
Keyword(s):  
Functional Characterization ◽  
Rna Polymerases ◽  
Eukaryotic Dna

scholarly journals Novel insertion and deletion mutants of RpoB that render Mycobacterium smegmatis RNA polymerase resistant to rifampicin-mediated inhibition of transcription

Microbiology ◽  
2010 ◽  
Vol 156 (5) ◽  
pp. 1565-1573 ◽  
Author(s):  
Vidyasagar Malshetty ◽  
Krishna Kurthkoti ◽  
Arnab China ◽  
Bratati Mallick ◽  
Subburaj Yamunadevi ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Mycobacterium Smegmatis ◽  
Three Dimensional ◽  
Rna Polymerases ◽  
Dimensional Structure ◽  
Deletion Mutants ◽  
Insertion And Deletion ◽  
Calf Thymus ◽  
Specific Activities ◽  
Spatial Positioning

The startling increase in the occurrence of rifampicin (Rif) resistance in the clinical isolates of Mycobacterium tuberculosis worldwide is posing a serious concern to tuberculosis management. The majority of Rif resistance in bacteria arises from mutations in the RpoB subunit of the RNA polymerase. We isolated M. smegmatis strains harbouring either an insertion (6 aa) or a deletion (10 aa) in their RpoB proteins. Although these strains showed a compromised fitness for growth in 7H9 Middlebrook medium, their resistance to Rif was remarkably high. The attenuated growth of the strains correlated with decreased specific activities of the RNA polymerases from the mutants. While the RNA polymerases from the parent or a mutant strain (harbouring a frequently occurring mutation, H442Y, in RpoB) were susceptible to Rif-mediated inhibition of transcription from calf thymus DNA, those from the insertion and deletion mutants were essentially refractory to such inhibition. Three-dimensional structure modelling revealed that the RpoB amino acids that interact with Rif are either deleted or unable to interact with Rif due to their unsuitable spatial positioning in these mutants. We discuss possible uses of the RpoB mutants in studying transcriptional regulation in mycobacteria and as potential targets for drug design.

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