J. Biol. Chem., Vol. 264, Issue 17, 9768-9771, 06, 1989
Canavanine incorporation into the antibacterial proteins of the fly, Phormia terranovae (Diptera), and its effect on biological activity
GA Rosenthal, J Lambert and D Hoffmann
T. H. Morgan School of Biological Sciences, Lexington, Kentucky.
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.
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