Canavanine incorporation into the antibacterial proteins of the fly, Phormia terranovae (Diptera), and its effect on biological activity.
In response to microbial infection or mechanical injury, larvae of the fly, Phormia terranovae (Diptera), can induce de novo production of a group of antibacterial proteins including: peak I protein, diptericin A, diptericin B, diptericin C, and peak V protein. Administration of L-canavanine at the time of mechanical injury results in the incorporation of this arginine antagonist into these proteins. Canavanine replacement for arginine causes a total loss of detectable antibacterial activity for diptericin B and diptericin C, whereas diptericin A and peak V protein are severely inhibited. This loss in biological activity occurs in spite of the fact that canavanine stimulates induced protein synthesis. Analysis of the hydrolysate of diptericin A reveals that one-third of the 3 arginyl residues are replaced by canavanine. This investigation provides the first evidence that canavanine incorporation into a protein can impair its function.
Rosenthal
G A
GA
T. H. Morgan School of Biological Sciences, Lexington, Kentucky.
Lambert
J
J
Hoffmann
D
D
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D002172:Canavanine / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004175:Diptera / Q000378:metabolism*; D029721:Drosophila Proteins; D004926:Escherichia coli / Q000187:drug effects; D006458:Hemolymph / Q000032:analysis; D007301:Insect Hormones / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology; D019476:Insect Proteins; D007700:Kinetics; D014176:Protein Biosynthesis; D011506:Proteins / Q000302:isolation & purification / Q000494:pharmacology
D000596:Amino Acids; D000900:Anti-Bacterial Agents; C054756:DptA protein, Drosophila; D029721:Drosophila Proteins; D007301:Insect Hormones; D019476:Insect Proteins; D011506:Proteins; D002172:Canavanine