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Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation

Author

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  • Malgorzata Dobosz-Bartoszek

    (University of Illinois at Chicago)

  • Mark H. Pinkerton

    (Rutgers—Robert Wood Johnson Medical School)

  • Zbyszek Otwinowski

    (University of Texas Southwestern Medical Center)

  • Srinivas Chakravarthy

    (Biophysics Collaborative Access Team/Illinois Institute of Technology, Sector 18ID, Advanced Photon Source)

  • Dieter Söll

    (and Chemistry, Yale University)

  • Paul R. Copeland

    (Rutgers—Robert Wood Johnson Medical School)

  • Miljan Simonović

    (University of Illinois at Chicago)

Abstract

Selenocysteine is the only proteinogenic amino acid encoded by a recoded in-frame UGA codon that does not operate as the canonical opal stop codon. A specialized translation elongation factor, eEFSec in eukaryotes and SelB in prokaryotes, promotes selenocysteine incorporation into selenoproteins by a still poorly understood mechanism. Our structural and biochemical results reveal that four domains of human eEFSec fold into a chalice-like structure that has similar binding affinities for GDP, GTP and other guanine nucleotides. Surprisingly, unlike in eEF1A and EF-Tu, the guanine nucleotide exchange does not cause a major conformational change in domain 1 of eEFSec, but instead induces a swing of domain 4. We propose that eEFSec employs a non-canonical mechanism involving the distinct C-terminal domain 4 for the release of the selenocysteinyl-tRNA during decoding on the ribosome.

Suggested Citation

  • Malgorzata Dobosz-Bartoszek & Mark H. Pinkerton & Zbyszek Otwinowski & Srinivas Chakravarthy & Dieter Söll & Paul R. Copeland & Miljan Simonović, 2016. "Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation," Nature Communications, Nature, vol. 7(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12941
    DOI: 10.1038/ncomms12941
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