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Plant Physiology 54:349-355 (1974)
© 1974 American Society of Plant Biologists

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Separation and Partial Characterization of Multiple Ribonucleic Acid Polymerases from Soybean Hypocotyl 1

Peter J. Rizzo, Joe H. Cherry, Karl Pedersen and Valgene L. Dunham2

a Department of Horticulture, Purdue University, West Lafayette, Indiana 47907

Two major peaks of RNA polymerase activity have been routinely separated by diethylaminoethyl cellulose chromatography following solubilization from soybean (Glycine max L. var. Wayne) chromatin. The relative amounts of these two peaks depend upon the manner in which the chromatin is purified. Pelleting the chromatin through dense sucrose solutions results in not only a loss of total solubilized RNA polymerase activity but also a selective loss of the {alpha}-amanitin-sensitive form of the enzyme. Peak I elutes from a diethylaminoethyl cellulose column at a KCl concentration of approximately 0.27 M, is insensitive to {alpha}-amanitin and rifamycin, and has Mg2+ + Mn2+ optima of 5 mM and 1.25 mM, respectively. The enzyme is inhibited by KCl concentrations of about 0.03 M or greater. Peak II elutes from the column at a KCl concentration of approximately 0.35 M, is sensitive to {alpha}-amanitin, insensitive to rifamycin, and has Mg2+ + Mn2+ optima of 2 mM and 1.0 mM, respectively. Activity is inhibited by KCl concentrations of about 0.06 M or greater. Both enzymes prefer denatured calf thymus DNA, but peak II exhibits a stronger preference.

2 Present address: State University of New York at Fredonia, Department of Biology, Fredonia, N. Y. 14063.

1 Journal Paper 5263 of the Purdue Agricultural Experimental Station. Supported by Grant 5 FO2 AM53070-02 to P.J.R. and by Grant RO1 ES 00551-03.






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Copyright © 1974 by the American Society of Plant Biologists