Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri

doi:10.1016/j.fsi.2007.06.010

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	Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri
	Li, Chenghua 1,2; Ni, Duojiao 1,2; Song, Linsheng 1; Zhao, Jianmin 1; Zhang, Huan 1; Li, Ling 1,2
	2008
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	24 期号:1 页码:26-34
文章类型	Article
摘要	Catalase is one of the central enzymes involved in scavenging the high level of reactive oxygen species (ROS) by degradation of hydrogen peroxide to oxygen and water. The full-length catalase cDNA of Zhikong scallop Chlamys farreri (denoted as CfCAT) was identified from hemocytes by expressed sequence tag (EST) and rapid amplification of cDNA ends (RACE) approaches. The nucleotide sequence of CfCAT cDNA consisted of 3146 bp with a 5' UTR of 103 bp, an unusually long 31 UTR of 1519 bp with a canonical polyadenylation signal sequence AATAAA and a potyA tail, and an open reading frame (ORF) of 1521 bp encoding a polypeptide of 507 amino acids with predicted molecular weight of 57.5 kDa. The deduced amino acid sequence of CfCAT has significant homology to catalases from animals, plants and bacteria. Several highly conserved motifs including the proximal heme-ligand signature sequence RLFSYNDTH, the proximal active site signature FNRERIPERVVHAKGGGA, and the three catalytic amino acid residues of His(72), Asn(145) and Tyr(355) were identified in the deduced amino acid sequence of CfCAT. The CfCAT was demonstrated to be a peroxisomal glycoprotein with two potential glycosylation sites and a peroxisome targeting signal of ANL that was consistent with human, mouse and rat catalases. The time-course expression of CfCAT in hemocytes was measured by quantitative real-time PCR. The expression of CfCAT increased gradually and reached the highest point at 12 h post-Vibrio infection, then recovered to the original level at 24 h. All these results indicate that CfCAT, a constitutive and inducible protein, is a member of the catalase family and is involved in the process against ROS in scallop. (c) 2007 Published by Elsevier Ltd.; Catalase is one of the central enzymes involved in scavenging the high level of reactive oxygen species (ROS) by degradation of hydrogen peroxide to oxygen and water. The full-length catalase cDNA of Zhikong scallop Chlamys farreri (denoted as CfCAT) was identified from hemocytes by expressed sequence tag (EST) and rapid amplification of cDNA ends (RACE) approaches. The nucleotide sequence of CfCAT cDNA consisted of 3146 bp with a 5' UTR of 103 bp, an unusually long 31 UTR of 1519 bp with a canonical polyadenylation signal sequence AATAAA and a potyA tail, and an open reading frame (ORF) of 1521 bp encoding a polypeptide of 507 amino acids with predicted molecular weight of 57.5 kDa. The deduced amino acid sequence of CfCAT has significant homology to catalases from animals, plants and bacteria. Several highly conserved motifs including the proximal heme-ligand signature sequence RLFSYNDTH, the proximal active site signature FNRERIPERVVHAKGGGA, and the three catalytic amino acid residues of His(72), Asn(145) and Tyr(355) were identified in the deduced amino acid sequence of CfCAT. The CfCAT was demonstrated to be a peroxisomal glycoprotein with two potential glycosylation sites and a peroxisome targeting signal of ANL that was consistent with human, mouse and rat catalases. The time-course expression of CfCAT in hemocytes was measured by quantitative real-time PCR. The expression of CfCAT increased gradually and reached the highest point at 12 h post-Vibrio infection, then recovered to the original level at 24 h. All these results indicate that CfCAT, a constitutive and inducible protein, is a member of the catalase family and is involved in the process against ROS in scallop. (c) 2007 Published by Elsevier Ltd.
关键词	Chlamys Farreri Catalase Gene Cloning Quantitative Real-time Pcr
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2007.06.010
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000253306700004
引用统计	被引频次：74[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/5590
专题	实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
第一作者单位	中国科学院海洋研究所
推荐引用方式 GB/T 7714	Li, Chenghua,Ni, Duojiao,Song, Linsheng,et al. Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri[J]. FISH & SHELLFISH IMMUNOLOGY,2008,24(1):26-34.
APA	Li, Chenghua,Ni, Duojiao,Song, Linsheng,Zhao, Jianmin,Zhang, Huan,&Li, Ling.(2008).Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri.FISH & SHELLFISH IMMUNOLOGY,24(1),26-34.
MLA	Li, Chenghua,et al."Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri".FISH & SHELLFISH IMMUNOLOGY 24.1(2008):26-34.

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