Phosphoprotein component of vaccinia virions.
The recent discovery of a protein kinase activity in vaccinia virions led us to search for a viral protein which is phosphorylated in vivo. Vaccinia virus was radioactively labeled by infecting cells in the presence of (32)P(1). A phosphoprotein was isolated from purified delipidated virions by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The phosphoprotein appeared to be a specific viral component induced after infection. More than 60% of the phosphoprotein was associated with viral cores. The electrophoretic mobility of the protein suggested that it has a molecular weight of 11,000 to 12,000. Phosphoserine was liberated by acid hydrolysis and identified by electrophoresis with known standards. Tryptic digests of the purified phosphoprotein were analyzed by two-dimensional electrophoresis and chromatography on thin-layer cellulose plates, and a single major phosphopeptide was resolved. The high selectivity of phosphorylation suggested that the process has a specific function.
D001345:Autoradiography; D002499:Centrifugation, Density Gradient; D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells; D006801:Humans; D010085:Oxidative Phosphorylation; D010748:Phosphopeptides / Q000032:analysis; D010750:Phosphoproteins / Q000032:analysis* / Q000302:isolation & purification; D010759:Phosphorus Isotopes; D012694:Serine / Q000032:analysis; D013912:Threonine / Q000032:analysis; D014316:Tritium; D014357:Trypsin; D014616:Vaccinia virus / Q000032:analysis* / Q000254:growth & development; D014764:Viral Proteins / Q000032:analysis* / Q000302:isolation & purification
D010748:Phosphopeptides; D010750:Phosphoproteins; D010759:Phosphorus Isotopes; D014764:Viral Proteins; D014316:Tritium; D013912:Threonine; D012694:Serine; D014357:Trypsin