Features of the pp60v-src carboxyl terminus that are required for transformation.
Analysis of the biological and biochemical activities of pp60recombinant-src proteins encoded by 12 carboxyl-terminal mutants showed that a wide family of alternate src carboxyl termini permit complete transforming and kinase activities. src proteins having carboxyl termini which are up to 10 amino acids longer than that of pp60c-src (17 amino acids longer than that of pp60v-src) still permit transformation. Transformation-positive mutations preserve leucine-516, a residue which is highly conserved in protein-tyrosine kinase sequences; removal causes in vivo protein instability. Successive deletion mutants show that this residue is at the boundary of a region required for kinase activity. pp60src which is truncated just outside this point still transforms cells and binds both pp50 and pp90 cellular proteins.
D000595:Amino Acid Sequence; D000818:Animals; D002471:Cell Transformation, Neoplastic; D051379:Mice; D009154:Mutation; D015688:Oncogene Protein pp60(v-src); D010750:Phosphoproteins / Q000378:metabolism; D010957:Plasmids; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D012191:Retroviridae Proteins / Q000032:analysis* / Q000235:genetics; D013329:Structure-Activity Relationship
D010750:Phosphoproteins; D012191:Retroviridae Proteins; D011505:Protein-Tyrosine Kinases; D015688:Oncogene Protein pp60(v-src)