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Nucleic Acids Research, 1988, Vol. 16, No. 12 5557-5568
© 1988

Articles

Expression of glutathione peroxidase I gene in selenium-deficient rats

Ambati P. Reddy1,2,3, Benjamin L. Hsu3, P.Sreenivasula Reddy2, Nan-qian Li2, Kedam Thyagaraju2, C.Channa Reddy2, Ming F. Tam3 and Chen-Pei D. Tu*,1,3

1Department of Molecular and Cell Biology, The Pennsylvania State University University Park, PA 16802, USA 2Department of Veterinary Science and Environmental Resources Research Institute, The Pennsylvania State University University Park, PA 16802, USA 3Institute of Molecular Biology Academia Sinica, 11529 Taipei, China

*To whom correspondence should be addressed

Received December 24, 1987. Revised April 28, 1988. Accepted April 28, 1988.

We have characterized a cDNA pGPX1211 encoding rat glutathione peroxidase I. The selenocysteine in the protein corresponded to a TGA codon in the coding region of the cDNA, similar to earlier findings in mouse and human genes, and a gene encoding the formate dehydrogenase from E. coli, another selenoenzyme. The rat GSH peroxidase I has a calculated subunit molecular weight of 22, 155 daltons and shares 95% and 86% sequence homology with the mouse and human subunits, respectively. The 3'-noncoding sequence (>930 bp) in pGPX1211 is much longer than that of the human sequences. We found that glutathione peroxidase I mRNA, but not the polypeptide, was expressed under nutritional stress of selenium deficiency where no glutathione peroxidase I activity can be detected. The failure of detecting any apoprotein for the glutathione peroxidase I under selenium deficiency and results published from other laboratories supports the proposal that selenium may be incorporated into the glutathione peroxidase I co-translationally.


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