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Title: MOLECULAR CLONING AND SEQUENCING OF HEMOGLOBIN-BETA GENE OF CHANNEL CATFISH, ICTALURUS PUNCTATUS RAFINESQUE

Author
item Yeh, Hung-Yueh
item Shoemaker, Craig
item Klesius, Phillip

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. Volume 32(1): 83-92.

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 catfish physiology, we cloned and sequenced the hemoglobin-' gene of channel catfish, Ictalurus 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 3D-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 Da. 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 3D-PSSM program displays that channel catfish hemoglobin-' is an alpha protein with eight '-helices, A ' H.

Technical Abstract: Hemoglobin-ÿ gene of channel catfish, Ictalurus punctatus, was cloned and sequenced. Total RNA from head kidneys was isolated, reverse transcribed and amplified. The sequence of the channel catfish hemoglobin-ÿ 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 Da. 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-ÿ 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 3D-PSSM program displays that channel catfish hemoglobin-ÿ is an alpha protein with eight ÿ-helices, A ' H.