ARS | Publication request: Molecular characterization, phylogenetic analysis and expression patterns of five protein arginine methyltransferase genes of channel catfish, Ictalurus punctatus (Rafinesque)

Submitted to: Fish Physiology and Biochemistry Journal
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: December 18, 2011
Publication Date: August 1, 2012
Citation: Yeh, H., Klesius, P.H. 2012. Molecular characterization, phylogenetic analysis and expression patterns of five protein arginine methyltransferase genes of channel catfish, Ictalurus punctatus (Rafinesque). Fish Physiology and Biochemistry Journal. 38:1083-1098.

Interpretive Summary: Protein arginine methyltransferases (PRMT) are a group of proteins that are able to add methyl molecules to the arginine residues in proteins. They are found in the living organisms, and play many important roles in normal cellular processes. In our study of channel catfish infection with Edwardsiella ictaluri, we found five PRMT genes (PRMT 1, 3, 4 and 5, and PRMT 4-like) were up-regulated at the early stage of infection. In this report, we sequenced and characterized these complimentary DNA (cDNA) transcripts. The cDNA transcripts have one open reading frames (ORF), which appear to encode 361, 587 and 458 amino acid residues, respectively, for the full-length nucleic acid sequences of channel catfish PRMT1, PRMT4 and PRMT4 variant. The partial ORF of PRMT3 and PRMT5 encode 292 and 563 amino acids, respectively. For expression profile, the channel catfish PRMT1 transcript was detected by RT-PCR in spleens, anterior kidneys, livers, intestines, skin and gills of fish examined. Except in liver, the PRMT3 transcript was detected in all catfish tissues examined. However, the PRMT4 cDNA was detected in livers from all three catfish and gills from two fish, but not other tissues. This study is related to the goal of ARS National Program 106-Aquaculture, Component 4C-Prevention of Diseases.

Technical Abstract: Protein arginine methylation, catalyzed by protein arginine methyltransferases (PRMT), has recently emerged as an important modification in the regulation of gene expression. In this communication, we identified and characterized the channel catfish orthologs to human PRMT 1, 3, 4 and 5, and PRMT4 like. Each PRMT nucleic acid sequence had an open reading frame (ORF) and 3’-untranslated regions. Each ORF appears to encode 361, 587 and 458 amino acid residues for PRMT1, PRMT4 and variant, respectively. The partial ORF of PRMT3 and PRMT5 encode 292 and 563 amino acids, respectively. By comparison with the human counterparts, each channel catfish PRMT also has conserved domains. For expression profile, the channel catfish PRMT1 transcript was detected by RT-PCR in spleens, anterior kidneys, livers, intestines, skin and gills of fish examines. Except in liver, the PRMT3 transcript was detected in all catfish tissues examined. However, the PRMT4 cDNA was detected in livers from all three catfish and gills from two fish, but not other tissues. This information will enable us to further elucidate PRMT functions in channel catfish.