Abstract
Mitochondrial capsule selenoprotein (MCS) has been known as a structural protein of the mitochondrial sheath in spermatoza. In the present study, a full-length cDNA encoding the MCS was first isolated from the testes of 10-week-old golden hamsters using a RACE (rapid amplification of cDNA ends) technique and its mRNA expression pattern was investigated from the hamster tissues by reverse transcription-polymerase chain reaction (RT-PCR) analysis. Hamster MCS cDNA was 820 bp long, including 24 bp of the 5'-untranslated region (UTR) and 243 bp of the 3'-UTR, and showed identity of 75.6% and 73.9% with mouse and rat MCS. According to the deduced amino acid (aa) sequence analysis, hamster MCS encoded a polypeptide of 184 aa, including a cysteine- and proline-rich domain which is the characteristic sequences of MCS, and contained 2 in-frame UGA codons for selenocysteine. Hamster MCS also shared aa identity of 64.4% with mouse MCS and contained an Arg-Lys-Ser-Thr-rich region in the N-terminus similar to the mitochondrial targeting signal. On the other hand, according to the RT-PCR analysis using the specific primers for hamster MCS, hamster MCS mRNA was expressed in various tissues as well as the testes. This finding indicates that MCS in hamster may have more than just a function of mitochondrial sheath formation of spermatozoa.
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