Physiological relevance of plant 2-Cys peroxiredoxin overoxidation level and oligomerization status
Physiological relevance of plant 2-Cys peroxiredoxin overoxidation level and oligomerization status
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DOI：
10.1111/pce.12596
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发表时间：
2016-01-01
影响因子：
7.3
通讯作者：
Rey, Pascal
中科院分区：
文献类型：
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作者：
Cerveau, Delphine;Ouahrani, Djelloul;Rey, Pascal
Peroxiredoxins是普遍存在的硫氧还蛋白依赖的过氧化物酶，在环境限制下，可能通过氧化还原依赖的构象开关发挥伴侣功能。在这项工作中，我们利用生化和遗传学的方法，旨在揭示调控植物体内2-半胱氨酸过氧化还蛋白(2-Cys PRX)氧化还原状态和构象的因素。在拟南芥中，我们发现在最佳的生长条件下，过氧化水平主要取决于硫氧还蛋白相关电子供体的可用性，而不是硫氧还蛋白，该酶能减少2-Cys PRX的过氧化形式。我们还观察到，在不同的生理温度、渗透和光胁迫条件下，2Cys Prx的过氧化水平和寡聚状态可以根据约束类型的不同而适度变化。此外，在水分胁迫下的拟南芥、大麦和马铃薯植株中没有观察到蛋白质构象的重大变化，而观察到物种依赖的过氧化上和下的变化。相反，在甲基紫精产生的严重氧化应激下，2-Cys-Prx的过氧化和寡聚都被强烈地诱导。根据这些数据，揭示了植物2-Cys Prx的寡聚状态没有表现出重要的变化，并且在生理相关的环境约束下与蛋白质的氧化还原状态没有紧密的联系，讨论了2-Cys Prx可能的植物功能。
Peroxiredoxins are ubiquitous thioredoxin-dependent peroxidases presumed to display, upon environmental constraints, a chaperone function resulting from a redox-dependent conformational switch. In this work, using biochemical and genetic approaches, we aimed to unravel the factors regulating the redox status and the conformation of the plastidial 2-Cys peroxiredoxin (2-Cys PRX) in plants. In Arabidopsis, we show that in optimal growth conditions, the overoxidation level mainly depends on the availability of thioredoxin-related electron donors, but not on sulfiredoxin, the enzyme reducing the 2-Cys PRX overoxidized form. We also observed that upon various physiological temperature, osmotic and light stress conditions, the overoxidation level and oligomerization status of 2Cys PRX can moderately vary depending on the constraint type. Further, no major change was noticed regarding protein conformation in water-stressed Arabidopsis, barley and potato plants, whereas species-dependent up-and down-variations in overoxidation were observed. In contrast, both 2-Cys PRX overoxidation and oligomerization were strongly induced during a severe oxidative stress generated by methyl viologen. From these data, revealing that the oligomerization status of plant 2-Cys PRX does not exhibit important variation and is not tightly linked to the protein redox status upon physiologically relevant environmental constraints, the possible in planta functions of 2-Cys PRX are discussed.