title: Phophorylation of polyoma and SV40 virus proteins.
abstract: The polypeptides of polyoma and SV40 virions are phosphorylated. An estimate of the amount of phosphorylation of the major virus capsid protein (VPI) has been made using two-dimensional gel electrophoresis to resolve phosphorylated from non-phosphorylated forms. The results suggest that in both polyoma and SV40 virions about 12% of VPI molecules are phosphorylated. In unassembled VPI molecules immunoprecipitated from extracts of infected cells the proportion is greater, about 33%. The possibility that phosphorylated VPI may form the penton proteins of the virus capsid is discussed.
mesh_terms: D002213:Capsid / Q000032:analysis*; D010455:Peptides / Q000032:analysis; D010710:Phosphates / Q000378:metabolism; D010750:Phosphoproteins / Q000032:analysis*; D011120:Polyomavirus / Q000378:metabolism / Q000648:ultrastructure*; D013539:Simian virus 40 / Q000378:metabolism / Q000648:ultrastructure*; D014764:Viral Proteins / Q000032:analysis*
chemical_list: D010455:Peptides; D010710:Phosphates; D010750:Phosphoproteins; D014764:Viral Proteins