RNA tumor virus phosphoproteins: primary structural analysis and identification of phosphopeptides.
Two-dimensional tryptic peptide mapping was used to compare the peptide sequences of the phosphoprotein (pp12) of cloned ecotropic and amphotropic wild mouse leukemia viruses, strains 1504 and 292. The maps of two ecotropic isolates were very similar to one another, as were the maps of two amphotropic isolates. There was also extensive similarity between the maps of this protein from ecotropic and amphotropic viruses, although characteristic peptide differences were readily recognized. These differences were consistent with the general type specificity of oncovirus phosphoproteins. The pp12 of the field isoalte of 292 virus contained five phosphopeptides, and the non-phosphorylated and variously phosphorylated species of this pp12 showed identical peptide maps, indicating differential phosphorylation of a single polypeptide.
D001483:Base Sequence; D009052:Leukemia Virus, Murine / Q000032:analysis*; D010748:Phosphopeptides / Q000032:analysis*; D010750:Phosphoproteins / Q000032:analysis*; D011487:Protein Conformation; D012190:Retroviridae / Q000032:analysis*; D014764:Viral Proteins / Q000032:analysis*
D010748:Phosphopeptides; D010750:Phosphoproteins; D014764:Viral Proteins