Abstract
UGA has a dual role in the genetic code serving as a signal for termination and a codon for selenocysteine (Sec). Sec appears to have been added to the already existing genetic code and its use has accumulated during evolution of eukaryotes culminating in vertebrates. Sec-containing proteins have diverse functions and lack a common amino acid motif or consensus sequence. Twenty two known eukaryotic selenoproteins may be subdivided into distinct selenoprotein groups on the basis of the location and functional properties of Sec. A set of criteria, designated Mammalian Selenoprotein Gene Signature (MSGS), allow recognition of selenoproteins through identification of SECIS elements and homology analyses of Sec-flanking areas. Identification of new selenoprotein sequences may lead to an understanding of many biological and health-related properties of selenium.
Keywords
- SECIS Element
- Selenoprotein Gene
- Phospholipid Hydroperoxide Glutathione Peroxidase
- Heterodisulfide Reductase
- Selenophosphate Synthetase
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Gladyshev, V.N. (2001). Identity, evolution and function of selenoproteins and selenoprotein genes. In: Hatfield, D.L. (eds) Selenium. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1609-5_9
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DOI: https://doi.org/10.1007/978-1-4615-1609-5_9
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5639-4
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