Back Cover: Rewiring Translation for Elongation Factor Tu-Dependent Selenocysteine Incorporation (Angew. Chem. Int. Ed. 5/2013)

Authors

  • Caroline Aldag,

    1. Department of Molecular Biophysics and Biochemistry, and Chemistry, Yale University, New Haven, CT 06520 (USA)
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    • These authors contributed equally to this work.

  • Markus J. Bröcker,

    1. Department of Molecular Biophysics and Biochemistry, and Chemistry, Yale University, New Haven, CT 06520 (USA)
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    • These authors contributed equally to this work.

  • Michael J. Hohn,

    1. Department of Molecular Biophysics and Biochemistry, and Chemistry, Yale University, New Haven, CT 06520 (USA)
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    • These authors contributed equally to this work.

  • Laure Prat,

    1. Department of Molecular Biophysics and Biochemistry, and Chemistry, Yale University, New Haven, CT 06520 (USA)
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    • These authors contributed equally to this work.

  • Gifty Hammond,

    1. Department of Molecular Biophysics and Biochemistry, and Chemistry, Yale University, New Haven, CT 06520 (USA)
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  • Abigail Plummer,

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

    Corresponding author
    1. Department of Molecular Biophysics and Biochemistry, and Chemistry, Yale University, New Haven, CT 06520 (USA)
    • Department of Molecular Biophysics and Biochemistry, and Chemistry, Yale University, New Haven, CT 06520 (USA)
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Abstract

original image

Synthetic tRNA for selenoprotein production is described by D. Söll et al. in their Communication on page 1441 ff. The tRNA is a substrate for three E. coli proteins: seryl-tRNA synthetase (SerRS), selenocysteine synthase (SelA) generating Sec-tRNAUTu, and EF-Tu for Sec-tRNAUTu transport to the ribosome, which allows site-specific Sec insertion into proteins. This system has general utility in protein engineering, molecular biology, and disease research.

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