Animal DNA-Dependent RNA Polymerases. 2. Purification of Calf-Thymus AI Enzyme

1972 ◽  
Vol 28 (2) ◽  
pp. 277-282 ◽  
Author(s):  
Francis Gissinger ◽  
Pierre Chambon
Keyword(s):  
1981 ◽  
Vol 46 (3) ◽  
pp. 673-677
Author(s):  
Květa Horská ◽  
Karel Šebesta

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.


1970 ◽  
Vol 38 (6) ◽  
pp. 1033-1040 ◽  
Author(s):  
M. Gniazdowski ◽  
J.L. Mandel ◽  
F. Gissinger ◽  
C. Kedinger ◽  
P. Chambon

1972 ◽  
Vol 28 (2) ◽  
pp. 269-276 ◽  
Author(s):  
Claude Kedinger ◽  
Francis Gissinger ◽  
Marek Gniazdowski ◽  
Jean-Louis Mandel ◽  
Pierre Chambon

Microbiology ◽  
2010 ◽  
Vol 156 (5) ◽  
pp. 1565-1573 ◽  
Author(s):  
Vidyasagar Malshetty ◽  
Krishna Kurthkoti ◽  
Arnab China ◽  
Bratati Mallick ◽  
Subburaj Yamunadevi ◽  
...  

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.


1970 ◽  
Vol 35 (0) ◽  
pp. 693-707 ◽  
Author(s):  
P. Chambon ◽  
F. Gissinger ◽  
J. L. Mandel ◽  
C. Kedinger ◽  
M. Gniazdowski ◽  
...  

1990 ◽  
Vol 55 (11) ◽  
pp. 2769-2780
Author(s):  
Aleš Cvekl ◽  
Květa Horská

A comparison was drawn between the action of Cibacron Blue F3GA on the enzymic activity of DNA-dependent RNA polymerases from different sources, e.g. Escherichia coli, calf thymus and wheat germ (polymerase II). Sensitivity towards this inhibitor was determined for polymer formation and primed abortive synthesis of trinucleotide UpApU. In case of E. coli polymerase and wheat germ polymerase II the dye inhibits both polymer formation and abortive synthesis. Calf thymus polymerase II is inhibited only in the polymerisation step. The primed initiation reaction was found to be resistant towards the dye. In case of E. coli polymerase and wheat germ polymerase II the sensitive step is the formation of internucleotide bond whereas in case of calf thymus polymerase II the translocation of the enzyme is influenced. An analysis of kinetic data indicates more than one binding site for the dye on RNA polymerase II from calf thymus and wheat germ. Cibacron blue does not inhibit specific transcription catalyzed by RNA polymerase III from human HeLa cells and mouse leukemia L1210 cells.


FEBS Letters ◽  
1973 ◽  
Vol 29 (2) ◽  
pp. 109-112 ◽  
Author(s):  
J.L. Mandel ◽  
C. Kedinger ◽  
F. Gissinger ◽  
P. Chambon ◽  
A.H. Fried

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