scholarly journals Octopine and nopaline metabolism in Agrobacterium tumefaciens and crown gall tumor cells: role of plasmid genes.

1977 ◽  
Vol 129 (1) ◽  
pp. 101-107 ◽  
Author(s):  
A L Montoya ◽  
M D Chilton ◽  
M P Gordon ◽  
D Sciaky ◽  
E W Nester
1957 ◽  
Vol 91 (860) ◽  
pp. 330-331 ◽  
Author(s):  
Richard M. Klein ◽  
Robert E. Beardsley

1976 ◽  
Vol 73 (10) ◽  
pp. 3562-3564 ◽  
Author(s):  
R. Turgeon ◽  
H. N. Wood ◽  
A. C. Braun

Planta Medica ◽  
1992 ◽  
Vol 58 (S 1) ◽  
pp. 603-603
Author(s):  
W. Pinkwart ◽  
B. Diettrich ◽  
M. Luckner

1963 ◽  
Vol 41 (7) ◽  
pp. 1503-1518 ◽  
Author(s):  
R. M. Hochster ◽  
V. M. Chang

The enzyme RNA polymerase has been partially purified from cell-free extracts of the crown-gall tumor-inducing organism Agrobacterium tumefaciens. The four triphosphates ATP, CTP, GTP, and UTP, manganese (or magnesium) ions, and DNA are all required for activity. DNA acts as a template in the formation of the new RNA molecule the base composition of which exactly mimics that of the particular DNA used. The dependence of the reaction on time, pH, and on the concentrations of nucleoside triphosphate, DNA, and protein has been worked out. The exact requirements of the entire system are delineated, the effect of physical alteration of the DNA used (heating, cooling, sonic oscillation) has been examined and a new observation made on the stimulation of DNA action by 1-minute sonic pretreatment.Actinomycin D is shown to inhibit the reaction completely at 2.8 × 10−5 M while atabrine, a new inhibitor, requires a concentration of 3.3 × 10−3 M under the conditions specified. Hydrolysis of the reaction product by means of a variety of procedures and other information obtained show that the reaction product is, indeed, RNA.The data reported herein are regarded as providing a satisfactory explanation for the mechanism of biosynthesis of at least one type of RNA (presumably "messenger" RNA) in A. tumefaciens.


1961 ◽  
Vol 39 (11) ◽  
pp. 1695-1704 ◽  
Author(s):  
A. Vardanis ◽  
R. M. Hochster

An investigation of the nucleotide specificity of the polynucleotide phosphorylase of Agrobacterium tumefaciens was undertaken, using the measurable increase in viscosity as an index of activity. It was found that ADP and CDP were polymerized readily and at approximately equal rates. The enzyme exhibited more moderate activity with UDP and was completely inactive with GDP. The ineffectiveness of the enzyme with mixtures of all four ribonucleoside diphosphates was traced to the ability of GDP to act as an inhibitor in the polymerization of the other diphosphates. Evidence is presented to show that the inhibition of poly A synthesis effected by GDP is competitive. On the basis of the results obtained it is concluded that the polynucleotide phosphorylase is not likely to be responsible for RNA synthesis in A. tumefaciens.


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