Get access

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)
    Search for more papers by this author
    • 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)
    Search for more papers by this author
    • 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)
    Search for more papers by this author
    • 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)
    Search for more papers by this author
    • 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)
    Search for more papers by this author
  • Abigail Plummer,

    1. Department of Molecular Biophysics and Biochemistry, and Chemistry, Yale University, New Haven, CT 06520 (USA)
    Search for more papers by this author
  • 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)
    Search for more papers by this author

  • 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

original image

Enjoying UTu in concert: A synthetic tRNA (tRNAUTu) was used as a substrate for three E. coli proteins: seryl-tRNA synthetase (SerRS) forming Ser-tRNAUTu, selenocysteine (Sec) synthase (SelA) generating Sec-tRNAUTu, and EF-Tu for Sec-tRNAUTu transport to the ribosome (see scheme). tRNAUTu can be used by the ribosome, thus allowing site-specific Sec insertion into proteins, including formate dehydrogenase H, selenoglutaredoxin, and glutathione peroxidase.

Get access to the full text of this article

Ancillary