Evidence for p15 cleavage site in myc-specific proteins of avian MC29 and OK10 viruses.
Myc-related proteins were precipitated from MC29 virus-transformed cells (PR-2) and from OK10 virus-transformed cells (9C) by anti-gag and anti-myc sera. Immunoprecipitates were cleaved with the avian retroviral protease p15 and the cleavage products analyzed in SDS-PAGE. Cleavage fragments of p110gag-myc (product of MC29 virus) and p58myc (product of OK10 virus) showed the presence of a p15 cleavage site within the myc-specific region. The site is missing in deletion mutants of MC29 virus.
D000818:Animals; D016282:Aspartic Acid Endopeptidases; D001354:Avian Leukosis Virus / Q000032:analysis / Q000235:genetics*; D001665:Binding Sites; D002460:Cell Line; D002472:Cell Transformation, Viral; D002645:Chickens; D015683:Gene Products, gag; D005796:Genes; D006868:Hydrolysis; D009856:Oncogene Proteins, Viral / Q000032:analysis*; D009857:Oncogenes; D010446:Peptide Fragments; D010447:Peptide Hydrolases; D011784:Quail; D012191:Retroviridae Proteins
D015683:Gene Products, gag; D009856:Oncogene Proteins, Viral; D010446:Peptide Fragments; D012191:Retroviridae Proteins; D010447:Peptide Hydrolases; D016282:Aspartic Acid Endopeptidases; C036946:protease p15