Skip to main content
ARS Home » Southeast Area » Auburn, Alabama » Aquatic Animal Health Research » Research » Publications at this Location » Publication #234912
Title: Characterization and tissue expression of channel catfish (Ictalurus punctatus, Rafinesque 1818) ubiquitin carboxyl-terminal hydrolase L5 (UCHL5) cDNA

Author
item Yeh, Hung-Yueh
item Klesius, Phillip

Submitted to: Molecular Biology Reports
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/24/2009
Publication Date: 3/6/2010
Citation: Yeh, H., Klesius, P.H. 2010. Characterization and tissue expression of channel catfish (Ictalurus punctatus, Rafinesque 1818) ubiquitin carboxyl-terminal hydrolase L5 (UCHL5) cDNA. Molecular Biology Reports. 37:1229-1234.

Interpretive Summary: Channel catfish is the most important aquacultural industry in the southeastern U.S. Like mammalian cells, channel catfish cells have several mechanisms for disposition of intracellular proteins. One of them is via the ubiquitin-proteasome cycle. This pathway needs many enzymes. Ubiquitin carboxy-terminal hydrolase L5 (UCT L5), which deubiquitylates the polyubiquitin chain into ubiquitin, is one of them involved in this pathway. In this communication, we report our results on studying this enzyme. The complete nucleic acid sequence of channel catfish UCT L5 complimentary DNA (cDNA) comprised of 1,357 nucleotides, including an open reading frame, which appears to encode a putative peptide of 329 amino acid residues. The estimated molecular weight and pI of this peptide are 37.6 kDa and 4.84, respectively. The degree of conservation of the channel catfish UCT L5 amino acid sequence in comparison to other species ranged from 79% to 92%. The channel catfish UCT L5 transcript was detected in spleen, head kidney, liver, intestine, skin and gill. This result provides important information for further elucidating UCT L5 in channel catfish.

Technical Abstract: The ubiquitin-proteasome cycle is a complex, non-lysosomal biochemical process for intracellular protein degradation. This process involves many enzymes. One of them is ubiquitin carboxy-terminal hydrolase L5 (UCT L5), which deubiquitylates the polyubiquitin chain into ubiquitin. In this report, we isolated, sequenced and characterized the channel catfish UCT L5 cDNA. The full-length nucleic acid sequence of channel catfish UCT L5 cDNA is comprised of 1,357 nucleotides, including an open reading frame, which appears to encode a putative peptide of 329 amino acid residues. The estimated molecular mass and pI of this peptide are 37.6 kDa and 4.84 at pH 7.0, respectively. The degree of conservation of the channel catfish UCT L5 amino acid sequence in comparison to other species ranged from 85% (vs. mouse) to 92% (vs. zebrafish and spotted green pufferfish). The channel catfish UCT L5 transcript was detected by RT-PCR in spleen, head kidney, liver, intestine, skin and gill, suggesting that the UCT L5 transcript is constitutively expressed. This research provides important information for further elucidating UCT L5 in the channel catfish ubiquitin-proteasome pathway.