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Phosphorylation of RNA Polymerases: Specific Association of Protein Kinase NII with RNA Polymerase I [and Discussion]
Kathleen M. Rose, D. A. Stetler, S. T. Jacob, L. A. Pinna and Kathleen M. Rose
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
Vol. 302, No. 1108, Biological Roles of Protein Phosphorylation (Jul. 5, 1983), pp. 135-142
Published by: Royal Society
Stable URL: http://www.jstor.org/stable/2396050
Page Count: 8
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The activities of the three DNA-dependent RNA polymerases from a rapidly growing rat tumour, Morris hepatoma 3924A, and from rat liver were examined. The activity of RNA polymerase I was higher in the tumour than in the liver. The enhanced capacity for RNA synthesis was a result of a higher concentration of polymerase I in the tumour as well as of an activation of this enzyme in vivo. The possibility that the high specific activity of the hepatoma polymerase I resulted from phosphorylation was investigated. Two major cyclic-AMP-independent nuclear casein kinases (NI and NII) were identified; the activity of protein kinase NII in the tumour was ten times that in liver. Protein kinase NII was capable of activating and phosphorylating RNA polymerase I in vitro. This kinase could also stimulate RNA polymerase II activity, although to a lesser extent than RNA polymerase I. RNA polymerase III was not affected by protein kinase NII. Protein kinase NII was tightly associated with polymerase I and was found even in purified preparations of the polymerase. Antibodies against both RNA polymerase I and protein kinase NII were present in sera of patients with certain rheumatic autoimmune diseases. These results imply that RNA polymerase I and protein kinase NII are in close association in vivo as well as in vitro and that polymerase phosphorylation may regulate the rate of ribosomal RNA synthesis in the cell.
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences © 1983 Royal Society