Characterization of an arginine-specific protein kinase tightly bound to rat liver DNA.
A new protein kinase has been characterized among the proteins tightly bound to rat liver DNA and released by DNase I and RNase A treatment. This enzyme was separated by gel filtration from this released material. Its apparent molecular mass was found to be 34 kDa and it is made of a single unit. The main characteristic of this protein kinase is that it is arginine-specific. Isolation of phosphoarginine required the use of proteolytic enzymes at alkaline pH since the phosphate bond is highly acid-labile. This protein kinase is able to autophosphorylate and to phosphorylate a single chromosomal protein of 11 kDa also tightly bound to DNA. It uses ATP and dATP as phosphate donors and is cAMP-independent. Its optimal activity requires Mn2+ ions. Vanadate, spermine and heparin have no effect on its activity.
D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002843:Chromatin / Q000201:enzymology; D002850:Chromatography, Gel; D004268:DNA-Binding Proteins / Q000302:isolation & purification*; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D002843:Chromatin; D004268:DNA-Binding Proteins; D001120:Arginine; D011494:Protein Kinases