L-canavanine incorporation into vitellogenin and macromolecular conformation.
L-Canavanine is a potentially deleterious arginine antimetabolite whose toxicity is expressed in canavanine-sensitive organisms ranging from viruses to humans. Canavanine, a substrate for arginyl-tRNA synthetase, is incorporated into nascent polypeptide chains in place of arginine. This substitution results in the production of structurally aberrant, canavanyl proteins. Chemical, physical, and immunological studies of native and canavanine-containing vitellogenin obtained from female migratory locusts (Locusta migratoria migratorioides (Orthoptera] provide the first experimental evidence that canavanine can disrupt the tertiary and/or quaternary structure that yields the three-dimensional conformation unique to the protein. These findings enhance our understanding of the biochemical basis for canavanine's antimetabolic and potent insecticidal properties.
T. H. Morgan School of Biological Sciences, University of Kentucky, Lexington 40506-0225.
G A
GA
Rosenthal
J M
JM
Reichhart
J A
JA
Hoffmann
D000818:Animals; D000911:Antibodies, Monoclonal; D002172:Canavanine / Q000378:metabolism*; D006110:Grasshoppers / Q000378:metabolism; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D014819:Vitellogenins / Q000096:biosynthesis* / Q000302:isolation & purification
D000911:Antibodies, Monoclonal; D014819:Vitellogenins; D002172:Canavanine