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Nucleic Acids Research Advance Access originally published online on August 3, 2009
Nucleic Acids Research 2009 37(17):5868-5880; doi:10.1093/nar/gkp635
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Nucleic Acids Research, 2009, Vol. 37, No. 17 5868-5880
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Novel structural determinants in human SECIS elements modulate the translational recoding of UGA as selenocysteine

Lynda Latrèche1,2, Olivier Jean-Jean2, Donna M. Driscoll3,4 and Laurent Chavatte1,3,*

1Centre de recherche de Gif-sur-Yvette, FRC 3115. Centre de Génétique Moléculaire, CNRS, FRE 3144, Gif-sur-Yvette, 2UPMC Univ Paris 06, FRE 3207, CNRS, F-75005 Paris, France, 3Department of Cell Biology, Lerner Research Institute, Cleveland Clinic Foundation and 4Department of Molecular Medicine, Cleveland Clinic Lerner College of Medicine of Case Western Reserve University, Cleveland, OH 44195, USA

*To whom correspondence should be addressed. Tel: (33) 1 69 82 32 13; Fax: (33) 1 69 82 31 40; Email: laurent.chavatte{at}cgm.cnrs-gif.fr

Received June 8, 2009. Revised July 15, 2009. Accepted July 16, 2009.

The selenocysteine insertion sequence (SECIS) element directs the translational recoding of UGA as selenocysteine. In eukaryotes, the SECIS is located downstream of the UGA codon in the 3'-UTR of the selenoprotein mRNA. Despite poor sequence conservation, all SECIS elements form a similar stem-loop structure containing a putative kink-turn motif. We functionally characterized the 26 SECIS elements encoded in the human genome. Surprisingly, the SECIS elements displayed a wide range of UGA recoding activities, spanning several 1000-fold in vivo and several 100-fold in vitro. The difference in activity between a representative strong and weak SECIS element was not explained by differential binding affinity of SECIS binding Protein 2, a limiting factor for selenocysteine incorporation. Using chimeric SECIS molecules, we identified the internal loop and helix 2, which flank the kink-turn motif, as critical determinants of UGA recoding activity. The simultaneous presence of a GC base pair in helix 2 and a U in the 5'-side of the internal loop was a statistically significant predictor of weak recoding activity. Thus, the SECIS contains intrinsic information that modulates selenocysteine incorporation efficiency.


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