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Published Online August 24, 2006
Science
DOI: 10.1126/science.1131981
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Reports
Submitted on June 30, 2006
Accepted on August 15, 2006
Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA
Christian B. F. Andersen 1,
Lionel Ballut 2,
Jesper S. Johansen 1,
Hala Chamieh 3,
Klaus H. Nielsen 1,
Cristiano L. P. Oliveira 4,
Jan Skov Pedersen 4,
Bertrand Séraphin 3,
Hervé Le Hir 3*,
Gregers Rom Andersen 1*
1 Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark; Centre for mRNP Biogenesis and Metabolism, University of Aarhus, Denmark.
2 epartment of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark; Equipe Labélisée La Ligue, Centre de Génétique Moléculaire, associé à l'Université Paris 6, CNRS UPR2167, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
3 Equipe Labélisée La Ligue, Centre de Génétique Moléculaire, associé à l'Université Paris 6, CNRS UPR2167, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
4 Centre for mRNP Biogenesis and Metabolism, University of Aarhus, Denmark; Department of Chemistry and iNANO Interdisciplinary Nanoscience Center, University of Aarhus, Langelandsgade 140, DK-8000 Aarhus, Denmark.
* To whom correspondence should be addressed.
Hervé Le Hir , E-mail: herve.lehir{at}cgm.cnrs-gif-fr
Gregers Rom Andersen , E-mail: gra{at}mb.au.dk
In higher eukaryotes a multiprotein exon junction complex is deposited on spliced mRNAs. The complex is organized around a stable core serving as a binding platform for numerous factors that influence mRNA function. Here, we present the crystal structure of a tetrameric exon junction core complex containing the DEAD-box ATPase eIF4AIII bound to an ATP analogue, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic. eIF4AIII interacts with the phosphate-ribose backbone of six consecutive nucleotides and prevents part of the bound RNA from being double stranded. The MAGOH and Y14 subunits lock eIF4AIII in a prehydrolysis state, and activation of the ATPase probably requires only modest conformational changes in eIF4AIII motif I.
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