EsTrx-2, the mitochondrial thioredoxin from Antarctic microcrustacean (Euphausia superba): Cloning and functional characterization
文献类型： 外文期刊
作者： Li, Fengmei 1 ; Liang, Yanjiao 1 ; Cai, Jinling 2 ; Shi, Yanjing 1 ; Ma, Liyan 3 ; Lu, Yongzhong 1 ;
作者机构： 1.Qingdao Univ Sci & Technol, Coll Marine Sci & Biol Engn, Shandong Prov Key Lab Biochem Engn, Qingdao 266042, Shandong, Peoples R China
2.Tianjin Univ Sci & Technol, Coll Chem Engn & Mat Sci, Tianjin Key Lab Marine Resources & Chem, Tianjin 300457, Peoples R China
3.Chinese Acad Fishery Sci, East China Sea Fisheries Res Inst, Shanghai 200090, Peoples R China
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.
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