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. 1986 Jan;83(1):14–18. doi: 10.1073/pnas.83.1.14

L-Canavanine and protein synthesis in the tobacco hornworm Manduca sexta.

G A Rosenthal, D L Dahlman
PMCID: PMC322781  PMID: 3455753

Abstract

L-Canavanine, a nonprotein amino acid of certain leguminous plants, manifests potent insecticidal properties in a canavanine-sensitive insect such as the tobacco hornworm Manduca sexta (L.) (Sphingidae). This arginine analog is activated and aminoacylated by arginyl-tRNA synthetase and incorporated into nascent polypeptide chains to create structurally aberrant, canavanine-containing proteins. Analysis of incorporation of [3H]leucine into protein in M. sexta larvae that had been injected with canavanine revealed that this arginine analog stimulates protein synthesis. During the first 3 hr after injection of canavanine, canavanine-mediated net stimulation of protein formation was readily discerned. Thereafter, the stimulation of protein synthesis appeared to be offset by the preferential degradation of anomalous proteins. Double-label protein-turnover experiments with larvae injected with [14C]canavanine- and [3H]arginine-containing hemolymph proteins showed that canavanine-containing proteins were degraded preferentially.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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