Purification and properties of a nuclear protein kinase associated with ribonucleic acid polymerase I

1978 ◽  
Vol 173 (3) ◽  
pp. 705.b3-705.b3
1978 ◽  
Vol 169 (2) ◽  
pp. 355-359 ◽  
Author(s):  
J Hirsch ◽  
O J Martelo

A cyclic AMP-dependent nuclear protein kinase was found to be closely associated with rat liver nucleolar RNA polymerase I throughout most of its purification. This protein kinase was purified to near homogeneity. It exhibits a number of unusual catalytic properties, including the inability to utilize Mn2+ when RNA polymerase is the substrate and the ability to phosphorylate both acidic and basic substrates. Phosphorylation of RNA polymerase I by this protein kinase results in the formation of phosphoester bonds characteristic of phosphoserine and phosphothreonine. Radioautography of polyacrylamide-gel electrophoretograms of the phosphorylated RNA polymerase I revealed that the 32P was located primarily on enzyme subunits SA1, SA3, SA5, and SA6 [nomenclature of Kedinger, Gissinger & Chambon (1974) Eur. J. Biochem, 44, 421-436].


1978 ◽  
Vol 253 (13) ◽  
pp. 4638-4641
Author(s):  
W. Thornburg ◽  
A.F. O'Malley ◽  
T.J. Lindell

1992 ◽  
Vol 267 (28) ◽  
pp. 19824-19828
Author(s):  
C Block ◽  
S Freyermuth ◽  
D Beyersmann ◽  
A.N. Malviya

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