Department of Biological Sciences, Texas Tech University, Box 4149, Lubbock, Texas 79409-3131.
Plant Physiol. 1992 Mar;98(3):1105-14. doi: 10.1104/pp.98.3.1105.
The aim of this study was to determine the response of photosynthetic carbon metabolism in spinach and bean to low temperature. (a) Exposure of warm-grown spinach and bean plants to 10 degrees C for 10 days resulted in increases in the total activities of a number of enzymes, including ribulose 1,5-bisphosphate carboxylase (Rubisco), stromal fructose 1,6 bisphosphatase (Fru 1,6-P(2)ase), sedoheptulose 1,7-bisphosphatase (Sed 1,7-P(2)ase), and the cytosolic Fru 1,6-P(2)ase. In spinach, but not bean, there was an increase in the total activity of sucrose-phosphate synthase. (b) The CO(2)-saturated rates of photosynthesis for the cold-acclimated spinach plants were 68% greater at 10 degrees C than those for warm-acclimated plants, whereas in bean, rates of photosynthesis at 10 degrees C were very low after exposure to low temperature. (c) When spinach leaf discs were transferred from 27 to 10 degrees C, the stromal Fru 1,6-P(2)ase and NADP-malate dehydrogenase were almost fully activated within 8 minutes, and Rubisco reached 90% of full activation within 15 minutes of transfer. An initial restriction of Calvin cycle fluxes was evident as an increase in the amounts of ribulose 1,5-bisphosphate, glycerate-3-phosphate, Fru 1,6-P(2), and Sed 1,7-P(2). In bean, activation of stromal Fru 1,6-P(2)ase was weak, whereas the activation state of Rubisco decreased during the first few minutes after transfer to low temperature. However, NADP-malate dehydrogenase became almost fully activated, showing that no loss of the capacity for reductive activation occurred. (d) Temperature compensation in spinach evidently involves increases in the capacities of a range of enzymes, achieved in the short term by an increase in activation state, whereas long-term acclimation is achieved by an increase in the maximum activities of enzymes. The inability of bean to activate fully certain Calvin cycle enzymes and sucrose-phosphate synthase, or to increase nonphotochemical quenching of chlorophyll fluorescence at 10 degrees C, may be factors contributing to its poor performance at low temperature.
本研究旨在确定菠菜和豆类光合作用碳代谢对低温的反应。(a)将温暖生长的菠菜和豆类植物暴露于 10°C 10 天,导致包括核酮糖 1,5-二磷酸羧化酶(Rubisco)、基质果糖 1,6-二磷酸酶(Fru 1,6-P(2)ase)、景天庚酮糖 1,7-二磷酸酶(Sed 1,7-P(2)ase)和细胞质果糖 1,6-P(2)ase 在内的多种酶的总活性增加。在菠菜中,但在豆类中,蔗糖磷酸合酶的总活性增加。(b)冷适应的菠菜植物在 10°C 时的 CO2 饱和光合作用速率比温暖适应的植物高 68%,而豆类在暴露于低温后,10°C 时的光合作用速率非常低。(c)当菠菜叶圆片从 27°C 转移到 10°C 时,基质 Fru 1,6-P(2)ase 和 NADP-苹果酸脱氢酶在 8 分钟内几乎完全激活,Rubisco 在转移后 15 分钟内达到 90%的完全激活。卡尔文循环通量的初始限制明显,表现在核酮糖 1,5-二磷酸、甘油酸-3-磷酸、Fru 1,6-P(2)和 Sed 1,7-P(2)的含量增加。在豆类中,基质 Fru 1,6-P(2)ase 的激活较弱,而 Rubisco 的激活状态在转移到低温后的最初几分钟内下降。然而,NADP-苹果酸脱氢酶几乎完全激活,表明没有发生还原激活能力的丧失。(d)菠菜中的温度补偿显然涉及一系列酶的容量增加,短期内通过激活状态增加来实现,而长期适应则通过酶的最大活性增加来实现。豆类不能充分激活某些卡尔文循环酶和蔗糖磷酸合酶,或不能增加叶绿素荧光的非光化学猝灭在 10°C 时,可能是其在低温下性能不佳的因素。