Threading the needle: Getting selenocysteine into proteins

Jesse Donovan, Paul Copeland

Research output: Contribution to journalReview article

52 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)881-892
Number of pages12
JournalAntioxidants and Redox Signaling
Volume12
Issue number7
DOIs
StatePublished - Apr 1 2010

Fingerprint

Selenocysteine
Needles
Proteins
Peptide Elongation Factors
DNA Transposable Elements
Nonsense Codon
Insertional Mutagenesis
Guanosine Triphosphate
Carrier Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

Cite this

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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 journalReview article

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