Properties of a human cytomegalovirus-induced protein kinase.
A human cytomegalovirus (HCMV)-induced polypeptide of 68,000 Da (p68) with protein kinase activity was identified using a monoclonal antibody (F6b) produced against HCMV-infected cell proteins. p68 was detected by immunoprecipitation from 3 to 120 hr after infection and was induced by several strains of human and not simian CMV. Protein kinase activity was associated almost exclusively with nuclear HCMV-induced p68. Enzyme activity with ATP and casein as phosphate donor and acceptor, respectively, exhibited an optimum pH between 6 and 6.5. It was Mg2+ dependent and cAMP independent. The KATPm of 45 microM at pH 6.5 indicated a relatively high affinity of p68 for the nucleotide. p68 also transferred phosphate to phosvitin and light chains of F6b, as well as autophosphorylating at threonine and serine residues.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D000911:Antibodies, Monoclonal; D000242:Cyclic AMP / Q000494:pharmacology; D003587:Cytomegalovirus / Q000201:enzymology* / Q000254:growth & development; D004790:Enzyme Induction; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D010766:Phosphorylation; D011494:Protein Kinases / Q000096:biosynthesis / Q000276:immunology / Q000378:metabolism*
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D008274:Magnesium