Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley
Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley
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DOI：
10.1104/pp.111.3.789
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发表时间：
1996-07-01
期刊：
影响因子：
7.4
通讯作者：
Wagner, E
中科院分区：
文献类型：
--
作者：
Desimone, M;Henke, A;Wagner, E
以大麦（Hordeum vulgare L.）叶绿体为材料，研究了氧化胁迫对1，5-二磷酸核酮糖羧化酶/加氧酶（Rubisco; EC 4.1.1.39）降解的影响。栽培品种安哥拉）。活性氧（AO）的产生通过改变光强度，氧气浓度，或添加除草剂或ADP-FeCl 3-抗坏血酸的培养基。氧化处理刺激协会的Rubisco与不溶性部分的叶绿体和大亚基（LSU）的部分蛋白水解。Rubisco的LSU的最突出的降解产物显示出36 kD的表观分子量。这些数据表明，在光系统I的O-2还原引发Rubisco降解的AO光生量的增加。AO介导的Rubisco变性和LSU的蛋白水解之间可能存在的关系进行了讨论。
The effects of oxidative stress on the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) were studied in isolated chloroplasts from barley (Hordeum vulgare L. cv Angora). Active oxygen (AO) was generated by varying the light intensity, the oxygen concentration, or the addition of herbicides or ADP-FeCl3-ascorbate to the medium. Oxidative treatments stimulated association of Rubisco with the insoluble fraction of chloroplasts and partial proteolysis of the large subunit (LSU). The most prominent degradation product of the LSU of Rubisco showed an apparent molecular mass of 36 kD. The data suggest that an increase in the amount of AO photogenerated by O-2 reduction at photosystem I triggers Rubisco degradation. A possible relationship between AO-mediated denaturation of Rubisco and proteolysis of the LSU is discussed.