Threading the needle: getting selenocysteine into proteins

Antioxid Redox Signal. 2010 Apr 1;12(7):881-92. doi: 10.1089/ars.2009.2878.

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-tRNA(Sec), 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Codon
  • Guanosine Triphosphate / metabolism
  • Humans
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Conformation
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Proteins / chemistry*
  • Proteins / metabolism
  • RNA / chemistry
  • RNA / genetics
  • RNA / metabolism
  • RNA Stability
  • RNA, Transfer, Amino Acyl / chemistry
  • RNA, Transfer, Amino Acyl / genetics
  • RNA, Transfer, Amino Acyl / metabolism
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism
  • Ribosomes / metabolism
  • Selenocysteine / metabolism*

Substances

  • Codon
  • Protein Isoforms
  • Proteins
  • RNA, Transfer, Amino Acyl
  • RNA-Binding Proteins
  • selenocysteine insertion sequence binding protein, mammalian
  • selenocysteinyl-tRNA
  • Selenocysteine
  • RNA
  • Guanosine Triphosphate