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 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Physiology
- Molecular Biology
- Clinical Biochemistry
- Cell Biology
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Threading the needle : Getting selenocysteine into proteins. / Donovan, Jesse; Copeland, Paul.
In: Antioxidants and Redox Signaling, Vol. 12, No. 7, 01.04.2010, p. 881-892.Research output: Contribution to journal › Review article
TY - JOUR
T1 - Threading the needle
T2 - Getting selenocysteine into proteins
AU - Donovan, Jesse
AU - Copeland, Paul
PY - 2010/4/1
Y1 - 2010/4/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77649258954&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77649258954&partnerID=8YFLogxK
U2 - 10.1089/ars.2009.2878
DO - 10.1089/ars.2009.2878
M3 - Review article
C2 - 19747061
AN - SCOPUS:77649258954
VL - 12
SP - 881
EP - 892
JO - Antioxidants and Redox Signaling
JF - Antioxidants and Redox Signaling
SN - 1523-0864
IS - 7
ER -