Molecular cloning and expression of gene fragments from corynebacteriophage beta encoding enzymatically active peptides of diphtheria toxin.
Two restriction fragments from corynebacteriophage beta vir tox+ that encode peptides similar to diphtheria toxin fragment A and the chain termination fragment, CRM45, have been cloned into Escherichia coli in plasmid pBR322. Clones containing the recombinant plasmids produced gene products that were active in catalyzing the ADP ribosylation of elongation factor 2 and were reactive with diphtheria toxin antiserum. Toxin-related peptides were found primarily in the periplasmic compartment and were degraded to nonimmunoreactive forms within 1 to 2 h of synthesis. The expression of both gene fragments appears to have originated from the diphtheria toxin promoter.
D001435:Bacteriophages / Q000235:genetics*; D003001:Cloning, Molecular; D003353:Corynebacterium diphtheriae / Q000235:genetics*; D004262:DNA Restriction Enzymes; D004167:Diphtheria Toxin / Q000235:genetics* / Q000302:isolation & purification; D005796:Genes; D005798:Genes, Bacterial; D005814:Genes, Viral; D008970:Molecular Weight; D009713:Nucleotidyltransferases / Q000235:genetics / Q000302:isolation & purification; D011065:Poly(ADP-ribose) Polymerases
D004167:Diphtheria Toxin; D011065:Poly(ADP-ribose) Polymerases; D009713:Nucleotidyltransferases; D004262:DNA Restriction Enzymes