Studies on the subunit structure of wheat germ ribonucleic acid polymerase II

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Abstract
A rapid, high yield method for the large scale purification of homogeneous RNA polymerase II from wheat germ was previously presented, and now a detailed study of its subunit structure is reported. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate indicates that polypeptides with MW of 220,000, 140,000, 40,000, 27,000, 25,000, 21,000, 20,000, 17,800, 17,000 16,500, 16,000 and approximately 14,000 are associated with the enzyme. Two-dimensional polyacrylamide gel electrophoresis, by which the subunits were separated in the 1st dimension in the presence of 8 M urea at pH 8.7 and in the 2nd dimension in the presence of 0.1% sodium dodecyl sulfate, indicates that the 40,000 MW component is composed of 2 nearly identical polypeptides and that the low MW components (.ltoreq. 40,000) are acidic proteins except for the 25,000 MW polypeptide.