Expression of an Abelson murine leukemia virus-encoded protein in Escherichia coli causes extensive phosphorylation of tyrosine residues.
A segment of the Abelson murine leukemia virus (A-MuLV) genome was inserted into an Escherichia coli plasmid designed to allow the expression of the protein encoded by the viral gene. Bacteria expressing the A-MuLV-encoded protein were isolated; they had new phosphorylated proteins in which the phosphate was linked to tyrosine residues. These proteins included many that must be E. coli protein. One phosphotyrosine-containing protein of 62,000 molecular weight had reactivity with antiserum specific for authentic A-MuLV protein. The A-MuLV protein thus appears to be a tyrosine-specific protein kinase which is active in E. coli.
D000011:Abelson murine leukemia virus / Q000235:genetics*; D000596:Amino Acids / Q000032:analysis; D004262:DNA Restriction Enzymes; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D005814:Genes, Viral; D009052:Leukemia Virus, Murine / Q000235:genetics*; D008970:Molecular Weight; D010766:Phosphorylation; D010957:Plasmids; D014176:Protein Biosynthesis; D014443:Tyrosine; D014764:Viral Proteins / Q000235:genetics* / Q000302:isolation & purification
D000596:Amino Acids; D014764:Viral Proteins; D014443:Tyrosine; D004262:DNA Restriction Enzymes