title: Protein kinases associated with the adenovirus single-stranded DNA-binding protein.
abstract: Protein kinase activities copurifying with the 72000-Mr DNA-binding protein of adenovirus on DNA-cellulose chromatography and gel filtration in acrylamide/agarose have been partially characterized and purified. One of these kinases was found to phosphorylate efficiently the viral DNA-binding protein in vitro and to be stimulated severalfold by the addition of histones, protamine, or polyamines. The kinase does not, however, phosphorylate histones, protamine, casein, or phosvitin. A second protein kinase was also recovered from single-stranded DNA-cellulose which is able to phosphorylate the 72000-Mr DNA-binding protein, but which is inhibited by the addition of histones. Phosphorylation in vitro of the 72000-Mr DNA-binding protein from the ts125 mutants of adenovirus by the histone-stimulated protein kinase was found to be thermosensitive.
mesh_terms: D000256:Adenoviridae / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002413:Cations, Divalent / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism*; D004279:DNA, Viral / Q000378:metabolism*; D004268:DNA-Binding Proteins; D006657:Histones / Q000378:metabolism; D006801:Humans; D008970:Molecular Weight; D010766:Phosphorylation; D011073:Polyamines / Q000378:metabolism; D011479:Protamines / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D002413:Cations, Divalent; D004277:DNA, Single-Stranded; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D006657:Histones; D011073:Polyamines; D011479:Protamines; D011494:Protein Kinases