Molecular Cloning and Characterization of the Myostatin Gene in Croceine Croaker, Pseudosciaena crocea

Abstract

Myostatin (MSTN) is a negative regulator of skeletal muscle mass and has a potential application in aquaculture. We reported the characterization of the myostatin gene and its expression in the croceine croaker, Pseudosciaena crocea. The myostatin gene had three exons encoding 376 amino acids. The cDNA was 1,906 bp long with a 5'-UTR and 3'-UTR of 108 bp and 667 bp, respectively. A microsatellite sequence, CA(30) and CA(26) separated by TA, existed in the 3'-UTR. Intron I and II were 343 bp and 758 bp in length, respectively. The deduced amino acid sequence was highly conserved, and had more than 90% identical to shi drum, gilthead seabream, striped sea-bass, white perch, and white bass proteins. The myostatin of croceine croaker had a putative amino terminal signal sequence (residues 1-22), a transforming growth factor-beta (TGF-beta) propeptide domain (residues 41-256), a RXXR proteolytic processing site (RARR, residues 264-267, matching the RXXR consensus site), and a TGF-beta domain (residues 282-376). There were 13 conserved cysteine residues in croceine croaker myostatin, nine of which are common to all TGF-beta superfamily members. The most conserved region of vertebrate myostatins is the TGF-beta domain, which was the mature bioactive domain of the myostatin protein. The myostatin gene was expressed not only in the skeletal muscle, but also in the other tissues.