L-canavanine and protein synthesis in the tobacco hornworm Manduca sexta

Journal Article · Tue Dec 31 23:00:00 EST 1985 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.83.1.14· OSTI ID:6155889

Rosenthal, G A; Dahlman, D L

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 (TH)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 of degradation of anomalous proteins. Double-label protein-turnover experiments with larvae injected with ( UC)canavanine- and (TH)arginine-containing hemolymph proteins showed that canavanine-containing proteins were degraded preferentially.

• Research Organization: Univ. of Kentucky, Lexington
• OSTI ID: 6155889
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 83:1; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ANIMALS
ARGININE
ARTHROPODS
BIODEGRADATION
BIOSYNTHESIS
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
DECOMPOSITION
DOUBLE LABELLING
INSECTICIDES
INSECTS
INVERTEBRATES
LABELLED COMPOUNDS
LABELLING
LEUCINE
ORGANIC ACIDS
ORGANIC COMPOUNDS
PESTICIDES
PROTEINS
SYNTHESIS
TRITIUM COMPOUNDS