Phosphate acceptor amino acid residues in structural proteins of rhabdoviruses.
Partial acid hydrolysates of the [(32)P]phosphate- or [(3)H]serine-labeled proteins of purified vesicular stomatitis, rabies, Lagos bat, Mokola, or spring viremia of carp virions and of purified intracellular nucleocapsids of these viruses have been analyzed by paper electrophoresis for the presence of phosphorylated amino acids. Both phosphoserine and phosphothreonine, with the former predominant, were present in virion and nucleocapsid preparations that contained phosphoproteins. An exception was the fish rhabdovirus, which contained only phosphoserine. When vesicular stomatitis or rabies virus proteins were phosphorylated in a cell-free system by the virion-associated protein kinase and analyzed for the presence of phosphorylated amino acid residues, phosphoserine was again found to be more abundant than phosphothreonine. After in vitro protein phosphorylation, another phospho-compound, possibly a third phosphoamino acid, was detected in the partial acid hydrolysates of these viruses.
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002685:Chiroptera; D003530:Cyprinidae; D004590:Electrophoresis, Paper; D010710:Phosphates; D010761:Phosphorus Radioisotopes; D012328:RNA Viruses / Q000032:analysis*; D011820:Rabies virus / Q000032:analysis; D012694:Serine; D014316:Tritium; D014721:Vesicular stomatitis Indiana virus / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis*
D000596:Amino Acids; D010710:Phosphates; D010761:Phosphorus Radioisotopes; D014764:Viral Proteins; D014316:Tritium; D012694:Serine