Cloning and characterization of selenoprotein thioredoxin reductase gene in Haematococcus pluvialis

被引:7
作者
Zheng, Yihong [1 ]
Tao, Ming [1 ]
Li, Ze [1 ]
Hu, Zhangli [1 ]
机构
[1] Shenzhen Univ, Shenzhen Key Lab Marine Bioresource & Ecoenvironm, Guangdong Engn Res Ctr Marine Algal Biotechnol, Coll Life Sci & Oceanog, Shenzhen 518060, Peoples R China
来源
ALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS | 2016年 / 17卷
基金
中国国家自然科学基金;
关键词
Selenoprotein; Haematococcus pluvialis; cDNA cloning; Thioredoxin reductase; 21ST AMINO-ACID; SELENOCYSTEINE; SELENIUM; EXPRESSION; STRESS; CANCER;
D O I
10.1016/j.algal.2016.03.038
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Thioredoxin reductase (TR) as a selenoprotein is involved in many cellular processes and mainly serves as a key member of the thioredoxin system, which is a crucial antioxidant systemin defense against oxidative stress. We investigated selenoproteins in the important commercial microalgae Haematococcus pluvialis. HpTR1 was identified and its molecular properties were analyzed. The full-length cDNA of HpTR1 consists of 2506 base pairs encoding a putative 535-amino acid product. The conformation of HpTR1 has been characterized via sequence analysis and protein structure modelling. A comprehensive phylogenetic tree of TR1 in animals and algae was constructed, which provided an evolution history of selenoprotein from aquatic to terrestrial environment. The expression pattern of TR1 mRNA and TR activity assay indicate that Selenium is an important regulator of HpTR1 and plays different roles in a dosage dependent manner. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:97 / 104
页数:8
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