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

American Association for the Advancement of Science (AAAS) - Tập 313 Số 5795 - Trang 1968-1972 - 2006
Christian Brix Folsted Andersen1,2,3,4, Lionel Ballut1,2,3,4, Jesper Johansen1,2,3,4, Hala Chamieh1,2,3,4, Klaus Nielsen1,2,3,4, Cristiano L. P. Oliveira1,2,4, Jan Skov Pedersen1,2,4, Bertrand Séraphin1,2,3,4, Hervé Le Hir1,2,3,4, G.R. Andersen1,2,3,4
1Centre for mRNP Biogenesis and Metabolism, University of Aarhus, DK-8000, Aarhus, Denmark
2Department of Chemistry and iNANO Interdisciplinary Nanoscience Center, University of Aarhus, DK-8000 Aarhus, Denmark
3Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus, Denmark
4Equipe Labélisée La Ligue, Centre de Génétique Moléculaire, associé à l'Université Paris 6, CNRS UPR2167, Avenue de la Terrasse, 91198 Gifsur-Yvette, France.

Tóm tắt

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.

Từ khóa


Tài liệu tham khảo

10.1093/emboj/19.24.6860

10.1016/j.ceb.2004.03.012

10.1038/nsmb990

10.1016/j.gene.2005.10.019

10.1126/science.291.5501.121

10.1126/science.1095596

10.1261/rna.2190706

Materials and methods are available as supporting material on Science Online.

10.1016/j.cell.2006.01.054

10.1074/jbc.M402754200

10.1073/pnas.97.24.13080

10.1016/S0960-9822(03)00328-2

10.1038/nsb926

10.1101/gad.260403

10.1016/j.molcel.2005.08.012

10.1074/jbc.M007560200

10.1016/S0021-9258(18)61430-9

A. Pause, N. Methot, N. Sonenberg, Mol. Cell. Biol.13, 6789 (1993).

10.1128/MCB.19.11.7336

10.1021/bi972430g

10.1016/j.ceb.2005.03.002

10.1016/j.ceb.2005.04.005

10.1016/S1097-2765(03)00142-4

10.1016/S0960-9822(02)00902-8

10.1093/emboj/cdf345

10.1101/gad.1335305

10.1038/sj.emboj.7600272

Single-letter abbreviations for the amino acid residues are as follows: A Ala; C Cys; D Asp; E Glu; F Phe; G Gly; H His; I Ile; K Lys; L Leu; M Met; N Asn; P Pro; Q Gln; R Arg; S Ser; T Thr; V Val; W Trp; and Y Tyr.

10.1038/sj.embor.7400091

We thank G. Hartvigsen for technical assistance; W. Merrick and E. Jankowsky for discussion and suggestions; T. Boesen F. Fredslund and the staffs at CASSIOPEIA European Synchrotron Radiation Facility and Swiss Light Source for help with data collection. G.R.A. and J.S.P. were supported by the Danish Natural Science Research Council and the Danish National Research Foundation. H.L.H. was supported by the CNRS the French Research Ministry (grant ACI-Jeunes Chercheurs) the Agence Nationale de la Recherche and the European Alternative Splicing Network. Structure factors and coordinates are deposited at the Protein Data Bank as entries 2HYI and 2HXY.

Thông tin
Thông tin xuất bản

American Association for the Advancement of Science (AAAS)

Tập 313 Số 5795

1968-1972

Thông tin tác giả