The Apparent Turnover of 1-Aminocyclopropane-1-Carboxylate Synthase in Tomato Cells Is Regulated by Protein Phosphorylation and Dephosphorylation

Open Access
Publisher Website
Google Scholar
Abstract
In suspension-cultured cells of tomato (Lycopersicon esculentum Mill.), the activity of 1-aminocyclopropane-1-carboxylate synthase (ACC-S) rapidly increases in response to fungal elicitors. The effect of inhibitors of protein kinases and protein phosphatases on the regulation of ACC-S was studied. K-252a, an inhibitor of protein kinases, prevented induction of the enzyme by elicitors and promoted its apparent turnover in elicitor-stimulated cells, causing a 50% loss of activity within 4 to 8 min in both the presence and absence of cycloheximide. Calyculin A, an inhibitor of protein phosphatases, caused a rapid increase of ACC-S in the absence of elicitors and an immediate acceleration of the rate of ACC-S increase in elicitor-stimulated cells. In the presence of cycloheximide there was no such increase, indicating that the effect depended on protein synthesis. Cordycepin, an inhibitor of mRNA synthesis, did not prevent the elicitor-induced increase in ACC-S activity but strongly reduced the K-252a-induced decay and the calyculin A-induced increase of its activity. In vitro, ACC-S activity was not affected by K-252a and calyculin A or by treatments with protein phosphatases. These results suggest that protein phosphorylation/dephosphorylation is involved in the regulation of ACC-S, not by regulating the catalytic activity itself but by controlling the rate of turnover of the enzyme.