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

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...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2006-09, Vol.313 (5795), p.1968-1972
Main Authors: Andersen, Christian B.F, Ballut, Lionel, Johansen, Jesper S, Chamieh, Hala, Nielsen, Klaus H, Oliveira, Cristiano L.P, Pedersen, Jan Skov, Séraphin, Bertrand, Le Hir, Hervé, Andersen, Gregers Rom
Format: Article
Language:English
Subjects:
RNA
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1131981