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Originally published in Science Express on 24 August 2006
Science 29 September 2006: Vol. 313. no. 5795, pp. 1968 - 1972
DOI: 10.1126/science.1131981
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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 Andersen1,2
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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