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Title: C DNA CLONING, CHARACTERIZATION AND EXPRESSION ANALYSIS OF CHANNEL CATFISH (ICTALURUS PUNCTATUS RAFINESQUE, 1818) PEROXIREDOXIN 6 GENE

Author
item Yeh, Hung-Yueh
item Klesius, Phillip

Submitted to: Fish Physiology and Biochemistry Journal
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/5/2007
Publication Date: 5/5/2007
Citation: Yeh, H., Klesius, P.H. 2007. c DNA cloning, characterization and expression analysis of channel catfish (Ictalurus punctatus Rafinesque, 1818). Fish Physiology and Biochemistry Journal. 33(3): 233-239.

Interpretive Summary: Channel catfish production is the largest aquacultural industry in the southeastern United States. Its annual output reaches 410 million dollars. In the course of studying Edwardsiella ictaluri pathogenesis, we cloned and sequenced the peroxiredoxin 6 gene (Prdx6) of channel catfish. The deduced amino acid sequence was compared with Prdx6 of other species deposited in the GenBank database. The sequence of the channel catfish Prdx6 consists of 1003 nucleotides. Analysis of the nucleotide sequence reveals one open reading frame and 5’- as well as 3’-untranslated regions. The open reading frame potentially encodes 223 amino acids with a calculated molecular mass of 24.6 Da. Unlike the counter part of bovine, the CC Prdx6 had four cysteine. Like the counter of mammalian Prdx6, CC Prdx6 contained reactive motifs that have peroxidase and phopholipase A2 activities. The CC Prdx6 transcript was detected in all analyzed tissues.

Technical Abstract: Peroxiredoxin 6 gene (Prdx6) of channel catfish, Ictalurus punctatus, was cloned and sequenced. Total RNA from channel catfish tissues was isolated, reverse transcribed and amplified. The sequence of the channel catfish Prdx6 gene consists of 1003 nucleotides. Analysis of the nucleotide sequence reveals one open reading frame and 5’- as well as 3’-untranslated regions. The open reading frame potentially encodes 223 amino acids with a calculated molecular mass of 24.6 kDa. Unlike the counter part of bovine, the CC Prdx6 had four cysteine. Like the counter of mammalian Prdx6, CC Prdx6 contained reactive motifs that have peroxidase and phopholipase A2 activities. The CC Prdx6 transcript was detected in all analyzed tissues.