title: Structure and function of the Abelson murine leukemia virus transforming gene.
abstract: The oncogene (v-abl) of A-MuLV is a fragment of a normal mouse gene. Only 1.2 kb on the 5'-end of the v-abl is sufficient to encode a tyrosine-specific protein kinase whose activity is important in transformation. This A-MuLV protein kinase can be active in E. coli and it phosphorylates bacterial proteins. The lack of discrimination in its selection for substrates is puzzling. Because of the demonstration of such promiscuity, the identification of physiologically-relevant phosphorylation events must rely on evidence of functional modification rather than physical modification of proteins.
mesh_terms: D000011:Abelson murine leukemia virus / Q000235:genetics*; D000818:Animals; D002472:Cell Transformation, Viral; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005814:Genes, Viral; D009052:Leukemia Virus, Murine / Q000235:genetics*; D051379:Mice / Q000235:genetics; D008957:Models, Genetic; D008979:Moloney murine leukemia virus / Q000235:genetics; D009857:Oncogenes; D011494:Protein Kinases / Q000235:genetics; D011505:Protein-Tyrosine Kinases; D014764:Viral Proteins / Q000235:genetics
chemical_list: D014764:Viral Proteins; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases