Cover Picture: Recoding the Genetic Code with Selenocysteine (Angew. Chem. Int. Ed. 1/2014)

Authors

  • Dr. Markus J. Bröcker,

    1. Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520 (USA)
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  • Joanne M. L. Ho,

    1. Department of Genetics, Harvard Medical School, Boston, MA 02115 (USA)
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  • Prof. George M. Church,

    1. Department of Genetics, Harvard Medical School, Boston, MA 02115 (USA)
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  • Prof. Dieter Söll,

    Corresponding author
    1. Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520 (USA)
    2. Department of Chemistry, Yale University, New Haven, CT 06520 (USA)
    • Dieter Söll, Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520 (USA)

      Patrick O'Donoghue, Departments of Biochemistry and Chemistry, Western University, London, ON N6A 5C1 (Canada)

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  • Prof. Patrick O'Donoghue

    Corresponding author
    1. Departments of Biochemistry and Chemistry, Western University, London, ON N6A 5C1 (Canada)
    • Dieter Söll, Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520 (USA)

      Patrick O'Donoghue, Departments of Biochemistry and Chemistry, Western University, London, ON N6A 5C1 (Canada)

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Abstract

original image

Named after Selene, goddess of the moon selenocysteine (Sec) is unique in its unrivaled catalytic power and its insertion into proteins by redefinition of specific UGA stop codons to Sec. In their Communication on page 319 ff., D. Söll, P. O'Donoghue et al. describe the engineering of the Sec-insertion machinery to redefine nearly all 64 codons. Here, the ring-shaped decameric selenocysteine synthase SeIA is essential in providing tRNA-bound Sec as the central building block for selenoprotein translation.

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