EsTrx-2, the mitochondrial thioredoxin from Antarctic microcrustacean (Euphausia superba): Cloning and functional characterization

文献类型： 外文期刊

第一作者： Li, Fengmei

作者： Li, Fengmei;Liang, Yanjiao;Shi, Yanjing;Lu, Yongzhong;Cai, Jinling;Ma, Liyan

作者机构：

关键词： Microcrustacean; Euphausia superba; Mitochondrial thioredoxin 2; Redox activity; Oxidative stress

期刊名称：COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY （ 影响因子：2.231； 五年影响因子：2.215 ）

ISSN： 1096-4959

年卷期： 2019 年 231 卷

页码：

收录情况： SCI

摘要： Thioredoxin system plays an important role in antioxidative stress, thioredoxin 2 (Trx2) being one of the most important components in the thioredoxin system. The full-length cDNA sequence of thioredoxin 2 from Euphausia superba (EsTrx2) is 1276 bp and contain a 5' untranslated region (UTR) of 94 bp, a 3' UTR of 741 bp and an open reading frame (ORF) of 441 bp, encoding a putative protein of 146 amino acids. Multiple sequence alignments have indicated that EsTrx2 possesses a conserved (-Cys-Gly-Pro-Cys-) CGPC redox-active site. EsTrx2 shares 62.3% identity with the swimming crab (Portunus trituberculatus) Trx2. The predicted three-dimensional structure of EsTrx2 consists of a thioredoxin fold. The high similarity and phylogenetic analysis have indicated that EsTrx2 is a member of the mitochondrial Trx2 sub-family. The recombinant EsTrx2 (rEsTrx2) was constructed and expressed in Escherichia coli BL21 (DE3). The rEsTrx2 protein showed high redox activity and antioxidant capacity at temperature from 4 to 37 degrees C. All results indicated that EsTrx2 was involved in the oxidative stress response of E. superba.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序