Phosphorylation of specific sites in the gag-myc polyproteins encoded by MC29-type viruses correlates with their transforming ability.
The putative transforming proteins of the four acute leukaemia viruses belonging to the MC29 subgroup were shown to be phosphorylated in vivo. Comparison of the MC29 and CM11 encoded phosphoproteins revealed identical tryptic phosphopeptide maps, with both the gag and myc domains being phosphorylated. In contrast, the MH2 phosphoprotein was only phosphorylated on the gag domain. Analysis of partial transformation-defective MC29 deletion mutants revealed that the deletions had removed the v-myc specific phosphopeptides. Phosphoamino acid analysis showed that these deleted phosphopeptides were phosphorylated on threonine. Moreover, a back mutant that had regained transforming ability had regained these phosphopeptides. These studies correlate the phosphorylation of the gag-myc protein with the transformation capability of the virus.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000956:Antigens, Viral / Q000235:genetics*; D002472:Cell Transformation, Viral; D003673:Defective Viruses / Q000235:genetics; D005347:Fibroblasts; D015683:Gene Products, gag; D009154:Mutation; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation; D011784:Quail; D012190:Retroviridae / Q000235:genetics*; D013045:Species Specificity; D014357:Trypsin; D014764:Viral Proteins / Q000235:genetics*
D000596:Amino Acids; D000956:Antigens, Viral; D015683:Gene Products, gag; D010446:Peptide Fragments; D014764:Viral Proteins; D014357:Trypsin