Expression and Characterization of a Protein Disulfide Isomerases in Maize (Zea Mays L.)
Expression and Characterization of a Protein Disulfide Isomerases in Maize (Zea Mays L.)
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发表时间：
2009
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通讯作者：
L. Ying
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作者：
L. Ying
蛋白质二硫键异构酶（PDI）在植物蛋白质折叠和氧化还原信号传导中发挥重要作用。本文分析了玉米 PDI 的特性和功能。玉米 PDI 基因包含 513 个氨基酸的开放阅读框，与小麦和水稻的 PDI 具有显着的保守性。所有 3 个 PDI 均具有两个硫氧还蛋白样活性位点 (CGHC) 和 C 末端内质网保留信号 (KDEL) 的典型结构。 Northern印迹表明，玉米PDI在发育中的种子中具有较高的表达水平，并且在脱水、寒冷、盐和脱落酸（ABA）胁迫下可以被强烈诱导。 PDI-GFP 融合蛋白的表达揭示了其在细胞核和细胞质区室中的定位。
Protein disulfide isomerases (PDIs) play an important roles in protein folding and redox signaling in plants. In this paper, we analyzed the characteristics and functions of a PDI from maize. The maize PDI gene included an open reading frame of 513 amino acids, which showed a significant conservation with PDIs from wheat and rice. All 3 PDIs have typical structures of two thioredoxin-like active sites (CGHC) and an endoplasmic reticulum-retention signal at its C-terminus (KDEL). Northern blotting showed that maize PDI had a higher expression level in developing seeds and could be strongly induced under dehydration, cold, salt and abscisic acid (ABA) stresses. The expression of PDI-GFP fusion protein revealed its localization in both nuclear and cytoplasm compartments.