Reports

Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA

Christian B. F. Andersen,^1,2* Lionel Ballut,^1,4* Jesper S. Johansen,^1,2 Hala Chamieh,⁴ Klaus H. Nielsen,^1,2 Cristiano L. P. Oliveira,^2,3 Jan Skov Pedersen,^2,3 Bertrand Séraphin,⁴ Hervé Le Hir,⁴ Gregers Rom Andersen^1,2

In higher eukaryotes, a multiprotein exon junction complex is deposited on spliced messenger RNAs. The complex is organized around a stable core, which serves as a binding platform for numerous factors that influence messenger RNA function. Here, we present the crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase (ATPase) eukaryotic initiation factor 4AIII (eIF4AIII) bound to an ATP analog, 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.

¹ Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus, Denmark.
² Centre for mRNP Biogenesis and Metabolism, University of Aarhus, DK-8000 Aarhus, Denmark.
³ Department of Chemistry and iNANO Interdisciplinary Nanoscience Center, University of Aarhus, DK-8000 Aarhus, Denmark.
⁴ Equipe Labélisée La Ligue, Centre de Génétique Moléculaire, associé à l'Université Paris 6, CNRS UPR2167, Avenue de la Terrasse, 91198 Gifsur-Yvette, France.

^* These authors contributed equally to this work.

To whom correspondence should be addressed. E-mail: gra{at}mb.au.dk (G.R.A.); herve.lehir{at}cgm.cnrs-gif.fr (H.L.H.).

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Z. Zhang and A. R. Krainer (2007)
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