Syntheses and stabilities of proteins related to the polyoma small T antigen in Escherichia coli.
We compared the syntheses and turnovers of two proteins related to the polyoma small T antigen synthesized in Escherichia coli from plasmids containing polyoma genomic segments joined to lac control elements. A protein with an authentic polyoma N terminus was more unstable than a protein with N-terminal amino acids derived from beta-galactosidase. Both were more unstable than most bacterial proteins.
D000956:Antigens, Viral / Q000032:analysis / Q000378:metabolism*; D000957:Antigens, Viral, Tumor; D003001:Cloning, Molecular; D004262:DNA Restriction Enzymes / Q000494:pharmacology; D004274:DNA, Recombinant; D015246:Deoxyribonuclease EcoRI; D004926:Escherichia coli / Q000276:immunology / Q000378:metabolism*; D009876:Operon; D010446:Peptide Fragments; D011120:Polyomavirus / Q000276:immunology; D014764:Viral Proteins / Q000378:metabolism
D000956:Antigens, Viral; D000957:Antigens, Viral, Tumor; D004274:DNA, Recombinant; D010446:Peptide Fragments; D014764:Viral Proteins; D004262:DNA Restriction Enzymes; D015246:Deoxyribonuclease EcoRI