Characterization of prosystemin expressed in the baculovirus/insect cell system reveals biological activity of the systemin precursor.
Tomato (Lycopersicon esculentum Mill.) prosystemin in fusion with a viral signal peptide was expressed in Sf21 insect cell cultures after infection with recombinant baculoviruses. Prosystemin was purified from culture supernatants and its identity was confirmed by N-terminal sequence and mass-spectral analyses. Recombinant prosystemin was found to be equally active as compared to systemin in inducing the expression of wound-response genes in tomato plants. In cultured cells of L. peruvianum, prosystemin elicited a rapid alkalinization of the growth medium. The timing and dose-dependence of the alkalinization response were found to be identical for prosystemin and systemin, respectively. Prosystemin-triggered defense responses were inhibited by a competitive antagonist of systemin activity, indicating that the systemin sequence within the primary structure of prosystemin determines its activity.[1]References
- Characterization of prosystemin expressed in the baculovirus/insect cell system reveals biological activity of the systemin precursor. Vetsch, M., Janzik, I., Schaller, A. Planta (2000) [Pubmed]
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