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

Malgorzata Dobosz-Bartoszek, Mark H. Pinkerton, Zbyszek Otwinowski, Srinivas Chakravarthy, Dieter Söll, Paul R. Copeland and Miljan Simonović ()
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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

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms12941

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