| First Author | Boschan C | Year | 2002 |
| Journal | Genomics | Volume | 79 |
| Issue | 3 | Pages | 387-94 |
| PubMed ID | 11863368 | Mgi Jnum | J:75163 |
| Mgi Id | MGI:2176012 | Doi | 10.1006/geno.2001.6715 |
| Citation | Boschan C, et al. (2002) Discovery of a functional retrotransposon of the murine phospholipid hydroperoxide glutathione peroxidase: chromosomal localization and tissue-specific expression pattern. Genomics 79(3):387-94 |
| abstractText | Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenoprotein capable of reducing toxic hydroperoxy ester lipids, has been implicated in antioxidative defense and spermatogenesis. Screening a murine genomic library, we isolated two recombinants (pseudogenes 1 and 2) containing retrotransposons for this enzyme. On comparison with the paralogous cDNA, pseudogene 1 contained only two silent nucleotide exchanges, and the 3prime prime or minute-untranslated region (3prime prime or minute-UTR) carrying the functionally important selenocysteine insertion sequence was free of mutations. This retrotransposon was found in various mouse strains and could be mapped to the region B2--B3 of chromosome 10. In vitro studies indicated significant promoter activity in the 5prime prime or minute-flanking region of pseudogene 1, and we observed a tissuespecific expression of this retrotransposon. In the submandibular gland. Most PHGPx transcripts originated from pseudogene 1. In contrast, pseudogene 2, containing numerous mutations in all parts of the retrotransposon, was not expressed in any tissue. It was mapped to region E3--E4 of chromosome 17, and we did not detect any promoter activity in its 5prime prime or minute-flanking region. These data indicate the existence of two retrotransposed PHGPx pseudogenes, one of which encodes a functional enzyme. This retrotransposon belongs to the rare group of pseudogenes that are tissue-specifically expressed under the control of captured regulatory elements, and it constitutes an example of evolutionarily acquired redundancy in gene expression. The results are important for the design of future knockout strategies aimed at investigating the biological role of this enzyme. |
