Abstract
The co-translational incorporation of selenocysteine (Sec) requires that UGA be recognized as a sense rather than a nonsense codon. This is accomplished by the concerted action of a Sec insertion sequence (SECIS) element, SECIS binding protein 2, and a ternary complex of the Sec specific elongation factor, Sec-tRNASec, and GTP. The mechanism by which they alter the canonical protein synthesis reaction has been elusive. Here we present an overview of the mechanistic perspective on Sec incorporation, highlighting recent advances in the field.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 881-892 |
| Number of pages | 12 |
| Journal | Antioxidants and Redox Signaling |
| Volume | 12 |
| Issue number | 7 |
| DOIs | |
| State | Published - Apr 1 2010 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Physiology
- Molecular Biology
- Clinical Biochemistry
- Cell Biology
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Cite this
Donovan, J., & Copeland, P. (2010). Threading the needle: Getting selenocysteine into proteins. Antioxidants and Redox Signaling, 12(7), 881-892. https://doi.org/10.1089/ars.2009.2878