High-level expression in Escherichia coli of the carboxy-terminal sequences of the avian myelocytomatosis virus (MC29) v-myc protein.

A plasmid, pJL6, was constructed that contains a unique ClaI site twelve codons beyond the bacteriophage lambda cII gene initiation codon. This site allowed us to fuse the carboxy-terminal sequences of the avian myelocytomatosis virus (MC29) v-myc gene to the amino-terminal portion of the cII gene. Transcription of the hybrid gene is controlled from the phage lambda pL promoter. When this promoter is derepressed, Escherichia coli cells harboring the chimeric plasmid produce a level of cII-myc fusion protein greater than 5% of total cellular protein. Antibodies raised by this protein immunoprecipitate the MC29 gag-myc gene product, P110gag-myc.