| 摘要: |
| 首次从海洋球石藻病毒(Emiliania huxleyi virus-EhV 99B1)中克隆了硫氧还蛋白(Trx)基因(该序列已提交GenBank, 登录号: GU109280)。系统进化关系分析表明: EhV99B1-Trx 与GenBank 中已报道的EhV86-Trx (NC_007346)有很高的同源性, 核酸及其推导的氨基酸序列的同源性分别为98%和100%, 而与其它物种的Trx 序列同源性仅为9.8%—18.8%。采用生物信息学方法和工具分析了EhV99B1-Trx 的生化参数, 预测了该蛋白的高级结构。结果表明: (1) EhV99B1-Trx 基因的开放阅读框全长591bp, 编码196 个氨基酸, 蛋白的相对分子量为22.1kDa, 理论等电点为5.27; (2) EhV-99B1-Trx N 端蛋白结构域具有保守的Cys-Gly-Pro-Cys (CGPC)硫氧还蛋白氧化还原活性位点氨基酸基序;(3) 对该蛋白二、三级结构分析预测结果进一步证实EhV99B1-Trx 基因编码的为一种新型的硫氧还蛋白家族成员。
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| 关键词: 海洋球石藻病毒(EhV), 硫氧还蛋白(Trx), 基因克隆及生物信息学分析 |
| DOI：10.11693/hyhz201002020020 |
| 分类号: |
| 基金项目:“十一五”国家科技支撑计划重大项目子课题, 2006BAD09A06 号; 集美大学中青年创新团队专项基金资助, 2008A002 号。 |
附件 |
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| CLONING AND BIOINFORMATIC ANALYSIS OF THIOREDOXIN-LIKE PROTEIN GENE (Trx) IN MARINE COCCOLITHOPHORID EMILIANIA HUXLEYI VIRUS |
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ZHANG Yan-Feng1, LIU Jing-Wen1, ZHANG Zhi-Lan1, DONG Shuang-Lin2
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1.College of Bio-Engineering, Jimei University;2.Key Laboratory of Mariculture Research, Ministry of Education, Ocean University of China
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| Abstract: |
| Thioredoxin (Trx) is a small ubiquitous protein that displays different functions mainly via redox-mediated processes. We here report the cloning and characters of a gene (EhV-Trx) coding for a novel thioredoxin-like protein in marine unicellular Emiliania huxleyi virus (EhV-99B1) (GenBank accession No.GU109280). EhV is the first virus-containing Trx gene reported. We also evaluated the phylogenetic relationships between EhV99B1-Trx and homologues from other organisms, showing a high identification with known Coccolithovirus EhV86-Trx gene (NC_007346) in 98% and 100% of nucleotide and deduced amino acid sequences, respectively. However, the EhV99B1-Trx had 9.8%—18.8% identity in amino acid sequence with other organisms. The secondary and the 3D structures of EhV99B1-Trx were predicted in bioinformatics. The results show that: (1) The thioredoxin gene had an open reading frame of 591bp, which contained
a deduced amino acid sequence with 196 residues, 22.1kDa in molecular mass and theoretical pI 5.27; (2) A conserved thioredoxin-like domain was detected in the N-terminal region of EhV-99B1 Trx, with a typical conserved Cys-Gly-Pro-Cys (CGPC) residue motif active site; (3) The predicted secondary and 3D structural modeling and folding patterns suggested that EhV99B1-Trx-like is identifiable as a new member of thioredoxin family. Therefore, this study provides novel insights into the relationship between Trx families and environment stress, as well as the interaction between EhVs infection and their hosts.
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| Key words: Emiliania huxleyi virus (EhV), Thioredoxin (Trx), Gene clone and bioinformatics |
