title: Analysis of gag-myc proteins of partially transformation-defective mutants of avian myelocytomatosis virus strain MC29 by in vitro cleavage with protease p15: indication for the presence of specific cleavage site p15 in the myc domain of fusion protein.
abstract: Gag-related proteins were immunoprecipitated from [35S]methionine-labelled cells of the PR-2 line which contained p110 protein as well as from quail cells transformed by deletion mutants 10A, 10C, and 10H of MC29 virus. Immunoprecipitates were incubated with oncoviral protease p15 and cleavage products were analyzed in SDS-PAGE. The major 56K fragment (F56) of p110 was further analyzed by tryptic peptide mapping. The results showed that except for the myc domain of p110, a portion of p27 is also present in F56. Cleavage of 100K, 95K, and 90K proteins coded by three MC29 deletion mutants resulted in major fragments 66K, 60K, and 56K, respectively. The existence of further cleavage fragments and presence of the p15 specific cleavage site in the myc domain of MC29 specific proteins is discussed.
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases; D001354:Avian Leukosis Virus / Q000235:genetics*; D009189:Avian Myeloblastosis Virus / Q000235:genetics*; D002460:Cell Line; D002472:Cell Transformation, Viral; D002645:Chickens; D002872:Chromosome Deletion; D015683:Gene Products, gag; D009154:Mutation; D010446:Peptide Fragments / Q000302:isolation & purification; D010447:Peptide Hydrolases; D011784:Quail; D014357:Trypsin; D014764:Viral Proteins / Q000235:genetics*
chemical_list: D015683:Gene Products, gag; D010446:Peptide Fragments; D014764:Viral Proteins; D010447:Peptide Hydrolases; D014357:Trypsin; D016282:Aspartic Acid Endopeptidases; C036946:protease p15