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ARS Home » Southeast Area » Athens, Georgia » U.S. National Poultry Research Center » Poultry Microbiological Safety and Processing Research Unit » Research » Publications at this Location » Publication #313583
Title: Molecular cloning and sequencing of hemoglobin-Beta gene of channel catfish, Ictalurus Punctatus Rafinesque

Author
item Yeh, Hung-Yueh
item SHOEMAKER, C - US Department Of Agriculture (USDA)
item KLESIUS, P - Retired ARS Employee

Submitted to: Fish Physiology and Biochemistry Journal
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/25/2006
Publication Date: 3/25/2006
Citation: Yeh, H., Shoemaker, C.A., Klesius, P.H. 2006. Molecular cloning and sequencing of hemoglobin-Beta gene of channel catfish, Ictalurus Punctatus Rafinesque. Fish Physiology and Biochemistry Journal. 83-92.

Interpretive Summary: Channel catfish production is the largest aquacultural industl)l in the southeastern United States. Its annual output reaches 410 million dollars. In the course of studying catfish physiology , we cloned and sequenced the hemoglobin-' gene of channel catfish, lctalurus punctatus. The deduced amino acid sequence was compared with hemoglobin-' of other species deposited in the GenBank database and its three-dimensional structure was predicted by the 30-PSSM program . The sequence of the channel catfish hemoglobin-' gene consists of 600 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 148 amino acids with a calculated molecular mass of 16.3 Oa. Overall, 22 amino acid residues were conserved throughout the sequences , including His64 and His93, the sites for iron-binding . The amino acid sequence of channel catfish hemoglobin-' shows 84% homology with that of Parasilurus asotus (both are in the order Siluriformes) . However, comparison with those of other fish species shows homology ranging from 53% to 68%. The structural analysis by the 30-PSSM program displays that channel catfish hemoglobin-'is an alpha protein with eight '-helices , A ' H.

Technical Abstract: : Hemoglobin-y gene of channel catfish , lctalurus punctatus, was cloned and sequenced . Total RNA from head kidneys was isolated, reverse transcribed and amplified . The sequence of the channel catfish hemoglobin-y gene consists of 600 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 148 amino acids with a calculated molecular mass of 16.3 Oa. Overall, 22 amino acid residues were conserved throughout the sequences , including His64 and His93, the sites for iron-binding . The amino acid sequence of channel catfish hemoglobin-y shows 84% homology with that of Parasilurus asotus (both are in the order Siluriformes) . However, compar ison with those of other fish species shows homology ranging from 53% to 68%. The structural analysis by the 30-PSSM program displays that channel catfish hemoglobin-y is an alpha protein with eighty-helices , A ' H.