Abstract
Selenoproteins are defined as proteins containing the 21st proteinogenic amino acid, selenocysteine (Sec). Sec is encoded by UGA (STOP) codons which are re-coded to Sec by the presence of a selenocysteine insertion sequence (SECIS) element in the 3’-untranslated region of selenoprotein mRNAs. The SECIS element is bound by several proteins, including SECIS-binding protein 2 (SBP2). Translation of selenoproteins critically depends on the integrity of the SECIS element – SBP2 interaction. Mutations in a SECIS element can abrogate expression of the respective selenoprotein. Mutations in SBP2 impinge on biosynthesis of a subset of selenoproteins and lead to a syndrome including hormonal, neurological, immunological symptoms as well as myopathy. Several other RNA-binding proteins are involved in selenoprotein translation and mediate the hierarchical response of selenoproteins to selenium deficiency. Global inhibition of selenoprotein translation is lethal in the mouse and hypomorphic mutations in selenocysteine synthase in humans leads to Progressive Cerebello Cerebral Atrophy, a neurodevelopmental and neurodegenerative disease in pediatric patients.
Keywords: Glutathione peroxidase, SepSecS, SECISBP2, selenocysteine, Selenoprotein biosynthesis, glutathione peroxidase 1, human genome, Selenoprotein, NMD, SECIS.
Current Protein & Peptide Science
Title:Post-Transcriptional Control of Selenoprotein Biosynthesis
Volume: 13 Issue: 4
Author(s): Sandra Seeher, Yassin Mahdi and Ulrich Schweizer
Affiliation:
Keywords: Glutathione peroxidase, SepSecS, SECISBP2, selenocysteine, Selenoprotein biosynthesis, glutathione peroxidase 1, human genome, Selenoprotein, NMD, SECIS.
Abstract: Selenoproteins are defined as proteins containing the 21st proteinogenic amino acid, selenocysteine (Sec). Sec is encoded by UGA (STOP) codons which are re-coded to Sec by the presence of a selenocysteine insertion sequence (SECIS) element in the 3’-untranslated region of selenoprotein mRNAs. The SECIS element is bound by several proteins, including SECIS-binding protein 2 (SBP2). Translation of selenoproteins critically depends on the integrity of the SECIS element – SBP2 interaction. Mutations in a SECIS element can abrogate expression of the respective selenoprotein. Mutations in SBP2 impinge on biosynthesis of a subset of selenoproteins and lead to a syndrome including hormonal, neurological, immunological symptoms as well as myopathy. Several other RNA-binding proteins are involved in selenoprotein translation and mediate the hierarchical response of selenoproteins to selenium deficiency. Global inhibition of selenoprotein translation is lethal in the mouse and hypomorphic mutations in selenocysteine synthase in humans leads to Progressive Cerebello Cerebral Atrophy, a neurodevelopmental and neurodegenerative disease in pediatric patients.
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Cite this article as:
Seeher Sandra, Mahdi Yassin and Schweizer Ulrich, Post-Transcriptional Control of Selenoprotein Biosynthesis, Current Protein & Peptide Science 2012; 13 (4) . https://dx.doi.org/10.2174/138920312801619448
DOI https://dx.doi.org/10.2174/138920312801619448 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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