Proteomic Analysis of Copper-Binding Proteins in Excess Copper-Stressed Roots of Two Rice (Oryza sativa L.) Varieties with Different Cu Tolerances.
Proteomic Analysis of Copper-Binding Proteins in Excess Copper-Stressed Roots of Two Rice (Oryza sativa L.) Varieties with Different Cu Tolerances.
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DOI：
10.1371/journal.pone.0125367
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发表时间：
2015
期刊：
影响因子：
3.7
通讯作者：
Shen Z
中科院分区：
文献类型：
--
作者：
Chen C;Song Y;Zhuang K;Li L;Xia Y;Shen Z
为了更好地了解植物对重金属胁迫的响应和耐受机制，采用蛋白质组学方法研究了耐铜和敏感铜水稻品种中cu结合蛋白的表达差异。采用一种新的IMAC方法从cu处理过的水稻根中分离cu结合蛋白，该方法在Cu-IMAC柱之前先用IDA-sepharose柱去除蛋白样品中的金属离子。在二维凝胶中可重复检测到300多个蛋白点。与对照组相比，35个蛋白点的变化强度大于1.5倍。24个蛋白质含有Smith等人报道的9个假定的金属结合基序中的一个或多个，19个蛋白质（点）含有Kung等人报道的前6个基序中的1到3个。耐铜品种B1139的7个蛋白斑点强度较铜敏感品种B1195显著升高（p<0.05）， 6个蛋白斑点在B1139中显著上调，而在B1195中未检测到。Cu胁迫下，B1139的4个蛋白点显著上调，而B1195的4个蛋白点不变。相比之下，B1195中有两个蛋白点显著下调，而B1139中没有变化。这些Cu-responsive蛋白质包括那些参与抗氧化防御和解毒(16点5日,21日,22日,28日,29日,33),发病机理(16点5日,21日,22日,28日,29日,33),调节基因转录(8点34),氨基酸合成(8点34),蛋白质合成,修改,运输和退化(点1、2、4、10、15、19日,30日,31日,32到35),细胞壁合成(现货14),分子信号(现货3),和盐压力(9点7日和27);与其他蛋白质一起，如假定的乙醛酸盐诱导蛋白，含有二聚体α - β桶结构域的蛋白和腺苷激酶样蛋白。我们的研究结果表明，这些蛋白与相关的生理过程一起，在过量铜的解毒和维持细胞稳态中发挥重要作用。
To better understand the mechanisms involved in the heavy metal stress response and tolerance in plants, a proteomic approach was used to investigate the differences in Cu-binding protein expression in Cu-tolerant and Cu-sensitive rice varieties. Cu-binding proteins from Cu-treated rice roots were separated using a new IMAC method in which an IDA-sepharose column was applied prior to the Cu-IMAC column to remove metal ions from protein samples. More than 300 protein spots were reproducibly detected in the 2D gel. Thirty-five protein spots exhibited changes greater than 1.5-fold in intensity compared to the control. Twenty-four proteins contained one or more of nine putative metal-binding motifs reported by Smith et al., and 19 proteins (spots) contained one to three of the top six motifs reported by Kung et al. The intensities of seven protein spots were increased in the Cu-tolerant variety B1139 compared to the Cu-sensitive variety B1195 (p<0.05) and six protein spots were markedly up-regulated in B1139, but not detectable in B1195. Four protein spots were significantly up-regulated in B1139, but unchanged in B1195 under Cu stress. In contrast, two protein spots were significantly down-regulated in B1195, but unchanged in B1139. These Cu-responsive proteins included those involved in antioxidant defense and detoxification (spots 5, 16, 21, 22, 28, 29 and 33), pathogenesis (spots 5, 16, 21, 22, 28, 29 and 33), regulation of gene transcription (spots 8 and 34), amino acid synthesis (spots 8 and 34), protein synthesis, modification, transport and degradation (spots 1, 2, 4, 10, 15, 19, 30, 31, 32 and 35), cell wall synthesis (spot 14), molecular signaling (spot 3), and salt stress (spots 7, 9 and 27); together with other proteins, such as a putative glyoxylate induced protein, proteins containing dimeric alpha-beta barrel domains, and adenosine kinase-like proteins. Our results suggest that these proteins, together with related physiological processes, play an important role in the detoxification of excess Cu and in maintaining cellular homeostasis.
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