Selenium pp 69-80 | Cite as

Towards a mechanism for selenocysteine incorporation in eukaryotes

  • John B. Mansell
  • Marla J. Berry

Abstract

The recent identification and cloning of two key proteins involved in the cotranslational incorporation of selenocysteine in eukaryotes has allowed the investigation of the mechanism by which the internal UGA codons of selenoprotein mRNAs are recoded from a canonical reading as termination, to encode selenocysteine. These proteins, selenocysteine insertion sequence (SECIS) binding protein 2 (SBP2), and eukaryotic selenocysteyl-tRNA[Ser]Sec-specific elongation factor (eEFsec), represent the first trans-acting protein factors clearly demonstrated to be involved in selenocysteine incorporation in eukaryotes. This chapter will focus on the cloning of eEFsec, in addition to presenting a discussion of prevalent current models describing the mechanism of selenocysteine incorporation in eukaryotes.

Keywords

Codon Glutathione Cysteine Electrophoresis Selenium 

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Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • John B. Mansell
    • 1
    • 2
  • Marla J. Berry
    • 1
    • 2
  1. 1.Thyroid Division, Brigham and Women’s HospitalHarvard Medical SchoolBostonUSA
  2. 2.Department of Biological Chemistry and Molecular PharmacologyHarvard Medical SchoolBostonUSA

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