The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility.
The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility.
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DOI：
10.1111/j.1399-3054.2008.01103.x
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发表时间：
2008-07
影响因子：
6.4
通讯作者：
E. Ströher;K. Dietz
中科院分区：
文献类型：
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作者：
E. Ströher;K. Dietz
巯基二硫化物氧化还原蛋白质组的动力学对细胞功能及其调控至关重要。蛋白质在氧化和还原状态下的迁移性改变允许基于质谱的鉴定那些经历主要构象变化的二硫醇蛋白质。对拟南芥叶绿体的类囊体结合、鲁米纳和核酮糖-1,5-二磷酸羧化酶/加氧酶（Rubisco）较少的基质亚蛋白质组部分进行了蛋白质组学分析。在49个已证实的多肽中，有22个新的氧化还原蛋白，以前未被报道为氧化还原蛋白组的一部分。受氧化还原作用影响的蛋白包括PsbA （D1）、PsaA1和PsaF、叶绿体单脱氢抗坏血酸还原酶和Deg1蛋白酶。重组Deg1和Deg2的蛋白水解活性显示出氧化还原依赖性。这些数据为叶绿体的氧化还原网络提供了新的见解。
The dynamics of the thiol-disulphide redox proteome is central to cell function and its regulation. Altered mobility of proteins in the oxidized and reduced state allows the MS-based identification of those thiol-disulphide proteins that undergo major conformational changes. A proteomic approach was taken with thylakoid-bound, luminal and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)-less stromal subproteome fractions of the chloroplast from Arabidopsis thaliana. Among the 49 verified polypeptides were 22 novel redox proteins, previously not reported as being part of the redox proteome. Among the redox-affected proteins were PsbA (D1), PsaA1 and PsaF, chloroplast monodehydroascorbate reductase and also the Deg1 protease. Recombinant Deg1 and Deg2 revealed redox dependence of their proteolytic activity. The data provide new insights into the redox network of the chloroplast.