The regulation of sucrose-phosphate synthase (SPS, E.C. 2.4.1.14), a key enzyme of sucrose synthesis, was investigated in wheat (Triticum aestivum L.) leaves. Wheat SPS was activated in the light, with an increased affinity for its substrates and the activator glucose-6-phosphate, reduced sensitivity to inhibition by Pi, but no change in maximum catalytic activity. Based on these properties, assays to measure the total activity and activation state of the enzyme were established and validated using several different wheat cultivars, grown under different environmental conditions. As found in previous studies on other species, e.g. spinach, activation appeared to be linked to the prevailing rate of photosynthesis rather than light per se. Long-term exposure to higher light levels increased total SPS activity in the leaves, and some experiments indicated that this response could occur within 1 h of exposure of low-light-grown plants to high light. However, activation of pre-existing enzyme was a more common short-term response to high light. Wheat, like many important cereal species, stores a large amount of sucrose in its leaves. In contrast with spinach, which stores more starch in its leaves, accumulation of sucrose in wheat leaves did not lead to inactivation of SPS or inhibition of sucrose synthesis. In conclusion, the mechanisms linking the rates of sucrose synthesis and photosynthetic CO2 fixation in wheat leaves appear to be similar to those in other species, but the mechanisms involved in short-term feedback inhibition of sucrose synthesis by sucrose, found in starch-storing species, are lacking in wheat.
Erratum to: Characterization of photosystem II heterogeneity in response to high salt stress in wheat leaves (Triticum aestivum)
