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
刊名	FISH & SHELLFISH IMMUNOLOGY
	2008
卷号	24 期号:1 页码:26-34
关键词	Chlamys Farreri Catalase Gene Cloning Quantitative Real-time Pcr
ISSN号	1050-4648
DOI	10.1016/j.fsi.2007.06.010
文献子类	Article
英文摘要	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.
学科主题	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
URL标识	查看原文
语种	英语
WOS记录号	WOS:000253306700004
公开日期	2010-12-24
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/5591]
专题	海洋研究所_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
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.