title: Isolation and biochemical characterization of partially transformation-defective mutants of avian myelocytomatosis virus strain MC29: localization of the mutation to the myc domain of the 110,000-dalton gag-myc polyprotein.
abstract: Recently, we isolated three mutants of MC29 virus which, although able to transform fibroblasts with the same efficiency as wild-type MC29, were 100-fold less efficient at transforming macrophages. In this study we found that MC29-transformed quail producer cell line Q10 was able to generate these partially transformation defective mutants at a high frequency. Using tryptic peptide mapping, we determined that the smaller gag-myc polyproteins encoded by the transformation-defective viruses had lost myc-specific tryptic peptides. This suggested that the mutations which resulted in the transformation-defective viruses being inefficient at transforming macrophages were located in the v-myc sequence and thus directly implicated v-myc and the gag-myc polyprotein in transformation by MC29.
mesh_terms: D000818:Animals; D001354:Avian Leukosis Virus / Q000235:genetics* / Q000302:isolation & purification; D002472:Cell Transformation, Viral; D003673:Defective Viruses / Q000235:genetics* / Q000302:isolation & purification; D005347:Fibroblasts / Q000382:microbiology; D005814:Genes, Viral; D008264:Macrophages / Q000382:microbiology; D009154:Mutation; D011784:Quail; D014764:Viral Proteins / Q000235:genetics; D014776:Virus Cultivation
chemical_list: D014764:Viral Proteins