Accuracy of wheat-germ RNA polymerase II. General enzymatic properties and effect of template conformational transition from right-handed B-DNA to left-handed Z-DNA

1992 ◽  
Vol 206 (1) ◽  
pp. 49-58 ◽  
Author(s):  
Laure MERCOYROL ◽  
Yves CORDA ◽  
Claudette JOB ◽  
Dominique JOB
Biochemistry ◽  
1988 ◽  
Vol 27 (17) ◽  
pp. 6371-6378 ◽  
Author(s):  
Dominique Job ◽  
Philippe Marmillot ◽  
Claudette Job ◽  
Thomas M. Jovin

1983 ◽  
Vol 2 (10) ◽  
pp. 1707-1714 ◽  
Author(s):  
R. Durand ◽  
C. Job ◽  
D.A. Zarling ◽  
M. Teissère ◽  
T.M. Jovin ◽  
...  

1992 ◽  
Vol 285 (1) ◽  
pp. 85-90 ◽  
Author(s):  
C Job ◽  
D Shire ◽  
V Sure ◽  
D Job

Wheat-germ RNA polymerase II is able to catalyse a DNA-dependent reaction of RNA synthesis in the presence of a high concentration (1 mg/ml) of the fungal toxin alpha-amanitin. This anomalous reaction is specifically directed by single-stranded or double-stranded homopolymer templates, such as poly(dC) or poly(dC).poly(dG), and occurs in the presence of either Mn2+ or Mg2+ as the bivalent metal cofactor. In contrast, the transcription of other synthetic templates, such as poly(dT), poly(dA).poly(dT) or poly[d(A-T)] is completely abolished in the presence of 1 microgram of alpha-amanitin/ml, in agreement with well-established biochemical properties of class II RNA polymerases. Size analysis of reaction products resulting from transcription of (dC)n templates of defined lengths suggests that polymerization of RNA chains proceeds through a slippage mechanism. The fact that alpha-amanitin does not impede this synthetic reaction implies that the amatoxin interferes with the translocation of wheat-germ RNA polymerase II along the DNA template.


1986 ◽  
Vol 14 (4) ◽  
pp. 1583-1597 ◽  
Author(s):  
Jacques Dietrich ◽  
Marcel Teissere ◽  
Claudette Job ◽  
Dominique Job

1988 ◽  
Vol 253 (1) ◽  
pp. 281-285 ◽  
Author(s):  
C Job ◽  
L De Mercoyrol ◽  
D Job

Progress curves of U-A-primed RNA synthesis catalysed by wheat-germ RNA polymerase II on a poly[d(A-T)] template exhibit a slow burst of activity. In contrast, the progress curves of single-step addition of UMP to U-A primer in the abortive elongation reaction do not exhibit the slow burst of activity. The correlation between the kinetic transient in the productive pathway of RNA synthesis and the rate of abortive elongation is suggestive of the occurrence of a slow conformational change of the transcription complex during the transition from abortive to productive elongation. The exceptional duration of the transient burst (in the region of 4 min) may suggest a transition of a hysteretic type.


1994 ◽  
Vol 311 (1) ◽  
pp. 35-41
Author(s):  
L. Cervoni ◽  
A. Ferraro ◽  
A. Giartosio ◽  
C.Q. Wang ◽  
C. Turano

1977 ◽  
Vol 74 (3) ◽  
pp. 1031-1038 ◽  
Author(s):  
Paul Petranyl ◽  
Jerome J. Jendrisak ◽  
Richard R. Burgess

1989 ◽  
Vol 54 (3) ◽  
pp. 811-818 ◽  
Author(s):  
Aleš Cvekl ◽  
Květa Horská ◽  
Karel Šebesta ◽  
Ivan Rosenberg ◽  
Antonín Holý

The elongation of dinucleotides ApU and UpA to trinucleotides ApUpA and UpApU by wheat germ RNA polymerase II was studied at a medium ionic strength (60 mM-KCl). The catalytic mechanism of the first internucleotide bond formation consists in the binding of the primer dinucleotide followed by the binding of NTP ("ordered bibi" reaction), i.e. by an analogous mechanism as found for RNA polymerase holoenzyme from E. coli. In further experiments phosphonate analogues of dinucleotides ApU and UpA were used as the priming dinucleotides. It was shown that analogues U(c)pA and Up(c)A are very poor primers for the synthesis of corresponding trinucleotides; the elongation of analogues A(c)pU and Ap(c)U was not observed at all. The comparison of kinetic constants Kia, KmA, KmB and Vmax as well as the substrate properties of phosphonate analogues indicates the increased specifity of the wheat germ RNA polymerase initiation binding site in comparison with the E. coli holoenzyme.


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