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Rewiring Translation for Elongation Factor Tu-Dependent Selenocysteine Incorporation

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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  • We thank David Lewin, Lynn Sherrer, and Patrick O’Donoghue for enthusiastic discussions, and Dan Su for experimental advice. We are grateful to TuKiet Lam and Edward Voss (W.M. Keck Foundation Biotechnology Resource Laboratory, Yale University) for their help with the FT-ICR mass spectral analyses. M.J.H. and M.J.B. acknowledge Feodor Lynen Postdoctoral Fellowships from the Alexander von Humboldt Foundation (Bonn (Germany)). C.A. was a Postdoctoral Fellow of the Swiss National Science Foundation. We gratefully acknowledge grant support from the Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy (DE-FG02-98ER20311; for funding the genetic experiments), from the National Institute of General Medical Sciences (GM 22854), and by DARPA contract N66001-12-C-4020.

Abstract

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Eine synthetische tRNA (tRNAUTu) wurde als Substrat für drei E.-coli-Proteine verwendet: Seryl-tRNA-Synthetase, die Ser-tRNAUTu bildet, Selenocystein(Sec)-Synthase, die Sec-tRNAUTu erzeugt, und EF-Tu für den Sec-tRNAUTu-Transport zum Ribosom (siehe Schema). tRNAUTu kann vom Ribosom verarbeitet werden, was die ortsspezifische Sec-Insertion in Proteine ermöglicht, darunter Formiat-Dehydrogenase H, Selenoglutaredoxin und Glutathion-Peroxidase.

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