Abstract:

Metallothioneins (MTs) was characterized by its low molecular weight (6 to 7 kDa), high metal content, high content of conserved cysteine(Cys) residues and absence of aromatic amino acids. In mammals there are four isoforms (MT-I—IV), MT-IV was expressed exclusively in stratified squamous epithelia. In this study, according to other animal MT-IV gene sequence from GenBank, a pair of special primers (MT-IV_SP1 and MT-IV_SP2) were designed for cloning the coding sequence of MT-IV from rumen organ in both sheep and goat. The MT-IV coding sequence in goat and sheep were 189bp, and be submitted to GenBank under Accession Numbers EF470251 and EF624067, respectively. Both goat and sheep MT-IV gene coded 62 AAs, including 20 Cys residues in sheep, 19 Cys residues in goat, the 61st conserved Cys was replaced by Trp in goat. MT-IV in goat and sheep both have characteristic Cys-x-Cys, Cys-x-y-Cys, and Cys-Cys sequences of MTs , where x and y were non-cysteine amino acids, no aromatic AAs, no cross membrane area, and no signal peptide, these information showed MT-IV in goat and sheep was a cytoplamic protein. The second structure of MT-IV was coil, except sheet structure in 7-9 AAs and 49-51AAs. The 3 dimension structure was composed by a-and b-domain, theβ-domain structure was same between sheep and goat, and same with other species, but a- domain structure in goat was difference with sheep and other species, because it less one Cys in goat than other animals,the structure change maybe alter the biological function, it is necessary to study furtherly.