Ferreira R M, Teixeira A R
Departamento de Botânica e Engenharia Biológica, Instituto Superior de Agronomia, Lisboa, Portugal.
J Biol Chem. 1992 Apr 15;267(11):7253-7.
Little is known about the degradation of the most abundant protein in nature, ribulose-bisphosphate carboxylase (RuBP carboxylase, EC 4.1.1.39), probably reflecting the fact that no stress situation has been identified capable of causing extensive RuBP carboxylase degradation without causing the death of the plant. We have subjected plants of Lemna minor L. to a variety of stress situations, nutritive deficiencies in particular, and have found a single condition--sulfur starvation--that caused almost complete degradation of RuBP carboxylase without causing plant death. Moreover, the enzyme was preferentially degraded under these conditions. However, when the plants were deprived of calcium, no RuBP carboxylase degradation was observed. Instead, the enzyme was oxidized and polymerized into high molecular mass aggregates. On the other hand, RuBP carboxylase shows an extreme stability when Lemna is deprived of some macronutrients (e.g. nitrogen, phosphorus, potassium, and magnesium) probably reflecting that this plant had to evolve in a way to cope with frequent shortages of such elements. The implications of these data for the role of RuBP carboxylase as a leaf storage protein are discussed.
关于自然界中最丰富的蛋白质——核酮糖-1,5-二磷酸羧化酶(RuBP羧化酶,EC 4.1.1.39)的降解情况,人们了解甚少,这可能反映出一个事实:尚未发现任何一种胁迫情况能够在不导致植物死亡的前提下,引起RuBP羧化酶的大量降解。我们让小浮萍(Lemna minor L.)植株经受了多种胁迫情况,尤其是营养缺乏,结果发现有一种情况——硫饥饿——能导致RuBP羧化酶几乎完全降解,且不会造成植物死亡。此外,在这些条件下,该酶会被优先降解。然而,当植株缺钙时,未观察到RuBP羧化酶的降解。相反,该酶被氧化并聚合成高分子量聚集体。另一方面,当小浮萍缺乏某些大量营养素(如氮、磷、钾和镁)时,RuBP羧化酶表现出极高的稳定性,这可能反映出这种植物必须以某种方式进化,以应对此类元素的频繁短缺。本文讨论了这些数据对于RuBP羧化酶作为叶片储存蛋白的作用的意义。