Protein Kinases Associated with the Adenovirus Single‐Stranded DNA‐Binding Protein

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Abstract
Protein kinase activities copurifying with the 72,000 MW DNA-binding protein of adenovirus on DNA-cellulose chromatography and gel filtration in acrylamide/agarose were partially characterized and purified. One of these kinases was found to efficiently phosphorylate the viral DNA-binding protein in vitro and to be stimulated severalfold by the addition of histones, protamine or polyamines. The kinase does not phosphorylate histones, protamine, casein or phosvitin. A 2nd protein kinase was also recovered from single-stranded DNA-cellulose which is able to phosphorylate the 72,000 MW DNA-binding protein but which is inhibited by the addition of histones. Phosphorylation in vitro of the 72,000 MW DNA-binding protein from the ts125 mutants of adenovirus by the histone-stimulated protein kinase was found to be thermosensitive.