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织锦巴菲蛤(Paphia textile)过氧化氢酶基因cDNA全长克隆、序列同源分析与组织表达
引用本文:武祥伟,李佳凯,谭茎,刘贤德.织锦巴菲蛤(Paphia textile)过氧化氢酶基因cDNA全长克隆、序列同源分析与组织表达[J].海洋学报(英文版),2016,35(8):65-73.
作者姓名:武祥伟  李佳凯  谭茎  刘贤德
作者单位:1 福建省海洋渔业资源与生态环境重点实验室, 集美大学水产学院, 厦门 361021;2 云南农业大学动物科学技术学院, 昆明 650201,1 福建省海洋渔业资源与生态环境重点实验室, 集美大学水产学院, 厦门 361021;2 云南农业大学动物科学技术学院, 昆明 650201,1 福建省海洋渔业资源与生态环境重点实验室, 集美大学水产学院, 厦门 361021;2 云南农业大学动物科学技术学院, 昆明 650201,1 福建省海洋渔业资源与生态环境重点实验室, 集美大学水产学院, 厦门 361021;2 云南农业大学动物科学技术学院, 昆明 650201
基金项目:The National Natural Science Foundation of China under contract No. 31172397; the New Century Excellent Talents of Fujian Province University under contract No. JA14167; the Open Research Fund Program of Fujian Provincial Key Laboratory of Marine Fishery Resources and Eco-environment under contract No. Z814041.
摘    要:Catalase is an important antioxidant protein that can protect organisms against various forms of oxidative damage by eliminating hydrogen peroxide. In this study, the catalase c DNA of Paphia textile(Pt CAT) was cloned using RTPCR and rapid amplification of c DNA ends(RACE). Pt CAT is 1 921 bp long and consists of a 5′-UTR of 50 bp, a 3′-UTR of 349 bp, and an ORF of 1 542 bp that encodes 513 amino acids with a molecular weight of 58.4 k D and an estimated isoelectric point of 8.2. Sequence alignment indicated that Pt CAT contained a highly conserved catalytic signature motif(~(61)FNRERIPERVVHAKGAG~(77)), a proximal heme-ligand signature sequence(~(352)RLFSYSDP~(359)), and three catalytic amino acid residues(H~(72), N~(145), and Y~(356)). Pt CAT also contains two putative N-glycosylation sites(~(34)NKT~(36) and ~(437)NFT~(439)) and a peroxisome-targeting signal(~(511)AQL~(513)). Furthermore, Pt CAT shares 53%–88% identity and 29%–89% similarity with other catalase amino acid sequences. Pt CAT m RNA was present in all tested organs, including the heart, digestive gland, adductor muscle, gonad, gill, and mantle, but its expression was highest in the digestive gland. High-temperature-induced stress produced two expression patterns of Pt CAT m RNA: first, an initial up-regulation followed by a down-regulation in the heart, digestive gland, and gonad and, second, consistent down-regulation in all other organs. These results demonstrate that Pt CAT is a typical member of the catalase family and might be involved in the responses to harmful environmental factors.

关 键 词:织锦巴菲蛤  过氧化氢酶(CAT)  克隆  序列分析  表达分析  高温胁迫
收稿时间:2015/5/26 0:00:00
修稿时间:2015/12/3 0:00:00

Molecular cloning, characterization and expression analysis of a catalase gene in Paphia textile
WU Xiangwei,LI Jiakai,TAN Jing and LIU Xiande.Molecular cloning, characterization and expression analysis of a catalase gene in Paphia textile[J].Acta Oceanologica Sinica,2016,35(8):65-73.
Authors:WU Xiangwei  LI Jiakai  TAN Jing and LIU Xiande
Institution:1 Fujian Provincial Key Laboratory of Marine Fishery Resources and Eco-environment, Fisheries College, Jimei University, Xiamen 361021, China;2 Animal Science and Technology College, Yunnan Agricultural University, Kunming 650201, China
Abstract:Catalase is an important antioxidant protein that can protect organisms against various forms of oxidative damage by eliminating hydrogen peroxide. In this study, the catalase cDNA of Paphia textile (PtCAT) was cloned using RTPCR and rapid amplification of cDNA ends (RACE). PtCAT is 1921 bp long and consists of a 5''-UTR of 50 bp, a 3''-UTR of 349 bp, and an ORF of 1 542 bp that encodes 513 amino acids with a molecular weight of 58.4 kD and an estimated isoelectric point of 8.2. Sequence alignment indicated that PtCAT contained a highly conserved catalytic signature motif (61FNRERIPERVVHAKGAG77), a proximal heme-ligand signature sequence (352RLFSYSDP359), and three catalytic amino acid residues (H72, N145, and Y356). PtCAT also contains two putative N-glycosylation sites (34NKT36 and 437439) and a peroxisome-targeting signal (511AQL513). Furthermore, PtCAT shares 53%-88% identity and 29%-89% similarity with other catalase amino acid sequences. PtCAT mRNA was present in all tested organs, including the heart, digestive gland, adductor muscle, gonad, gill, and mantle, but its expression was highest in the digestive gland. High-temperature-induced stress produced two expression patterns of PtCAT mRNA:first, an initial up-regulation followed by a down-regulation in the heart, digestive gland, and gonad and, second, consistent down-regulation in all other organs. These results demonstrate that PtCAT is a typical member of the catalase family and might be involved in the responses to harmful environmental factors.
Keywords:Paphia textile  catalase (CAT)  cloning  sequence analysis  expression analysis  high temperature stress
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