Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

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
Prev | Table of Contents | Next

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{dagger} Gregers Rom Andersen1,2{dagger}

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.

{dagger} 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.).

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: implications for DNA restriction and translocation activity.
N. T. Uyen, S.-Y. Park, J.-W. Choi, H.-J. Lee, K. Nishi, and J.-S. Kim (2009)
Nucleic Acids Res. 37, 6960-6969
   Abstract »    Full Text »    PDF »
The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core.
M. G. Rudolph and D. Klostermeier (2009)
RNA 15, 1993-2001
   Abstract »    Full Text »    PDF »
Remodeling of the pioneer translation initiation complex involves translation and the karyopherin importin {beta}.
H. Sato and L. E. Maquat (2009)
Genes & Dev. 23, 2537-2550
   Abstract »    Full Text »    PDF »
An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd.
M. N. Murphy, P. Gong, K. Ralto, L. Manelyte, N. J. Savery, and K. Theis (2009)
Nucleic Acids Res. 37, 6042-6053
   Abstract »    Full Text »    PDF »
SrmB, a DEAD-box helicase involved in Escherichia coli ribosome assembly, is specifically targeted to 23S rRNA in vivo.
D. Trubetskoy, F. Proux, F. Allemand, M. Dreyfus, and I. Iost (2009)
Nucleic Acids Res. 37, 6540-6549
   Abstract »    Full Text »    PDF »
Inhibition of Nonsense-mediated mRNA Decay by the Natural Product Pateamine A through Eukaryotic Initiation Factor 4AIII.
Y. Dang, W.-K. Low, J. Xu, N. H. Gehring, H. C. Dietz, D. Romo, and J. O. Liu (2009)
J. Biol. Chem. 284, 23613-23621
   Abstract »    Full Text »    PDF »
A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN.
A. R. Karow and D. Klostermeier (2009)
Nucleic Acids Res. 37, 4464-4471
   Abstract »    Full Text »    PDF »
Aberrant mRNA Transcripts and the Nonsense-Mediated Decay Proteins UPF2 and UPF3 Are Enriched in the Arabidopsis Nucleolus.
S. H. Kim, O. A. Koroleva, D. Lewandowska, A. F. Pendle, G. P. Clark, C. G. Simpson, P. J. Shaw, and J. W.S. Brown (2009)
PLANT CELL 21, 2045-2057
   Abstract »    Full Text »    PDF »
Dynamic Behavior of Arabidopsis eIF4A-III, Putative Core Protein of Exon Junction Complex: Fast Relocation to Nucleolus and Splicing Speckles under Hypoxia.
O.A. Koroleva, G. Calder, A.F. Pendle, S.H. Kim, D. Lewandowska, C.G. Simpson, I.M. Jones, J.W.S. Brown, and P.J. Shaw (2009)
PLANT CELL 21, 1592-1606
   Abstract »    Full Text »    PDF »
The DEXD/H-box RNA Helicase DDX19 Is Regulated by an {alpha}-Helical Switch.
R. Collins, T. Karlberg, L. Lehtio, P. Schutz, S. van den Berg, L.-G. Dahlgren, M. Hammarstrom, J. Weigelt, and H. Schuler (2009)
J. Biol. Chem. 284, 10296-10300
   Abstract »    Full Text »    PDF »
A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.
D. Klostermeier and M. G. Rudolph (2009)
Nucleic Acids Res. 37, 421-430
   Abstract »    Full Text »    PDF »
Mechanism of ATP turnover inhibition in the EJC.
K. H. Nielsen, H. Chamieh, C. B.F. Andersen, F. Fredslund, K. Hamborg, H. Le Hir, and G. R. Andersen (2009)
RNA 15, 67-75
   Abstract »    Full Text »    PDF »
ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding.
F. Liu, A. Putnam, and E. Jankowsky (2008)
PNAS 105, 20209-20214
   Abstract »    Full Text »    PDF »
DEAD-box proteins can completely separate an RNA duplex using a single ATP.
Y. Chen, J. P. Potratz, P. Tijerina, M. Del Campo, A. M. Lambowitz, and R. Russell (2008)
PNAS 105, 20203-20208
   Abstract »    Full Text »    PDF »
Flexibility in the site of exon junction complex deposition revealed by functional group and RNA secondary structure alterations in the splicing substrate.
D. M. Mishler, A. B. Christ, and J. A. Steitz (2008)
RNA 14, 2657-2670
   Abstract »    Full Text »    PDF »
Interactions between eIF4AI and its accessory factors eIF4B and eIF4H.
N. Rozovsky, A. C. Butterworth, and M. J. Moore (2008)
RNA 14, 2136-2148
   Abstract »    Full Text »    PDF »
The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity.
M. H. Linden, R. K. Hartmann, and D. Klostermeier (2008)
Nucleic Acids Res. 36, 5800-5811
   Abstract »    Full Text »    PDF »
A Proteomic Comparison of Immature and Mature Mouse Gonadotrophs Reveals Novel Differentially Expressed Nuclear Proteins that Regulate Gonadotropin Gene Transcription and RNA Splicing.
J. Feng, M. A. Lawson, and P. Melamed (2008)
Biol Reprod 79, 546-561
   Abstract »    Full Text »    PDF »
Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein-protein interactions.
P. Schutz, M. Bumann, A. E. Oberholzer, C. Bieniossek, H. Trachsel, M. Altmann, and U. Baumann (2008)
PNAS 105, 9564-9569
   Abstract »    Full Text »    PDF »
A Conserved Phenylalanine of Motif IV in Superfamily 2 Helicases Is Required for Cooperative, ATP-Dependent Binding of RNA Substrates in DEAD-Box Proteins.
J. Banroques, O. Cordin, M. Doere, P. Linder, and N. K. Tanner (2008)
Mol. Cell. Biol. 28, 3359-3371
   Abstract »    Full Text »    PDF »
Binding of ATP to UAP56 is necessary for mRNA export.
K. P. Kota, S. R. Wagner, E. Huerta, J. M. Underwood, and J. A. Nickerson (2008)
J. Cell Sci. 121, 1526-1537
   Abstract »    Full Text »    PDF »
Conformational changes of a Swi2/Snf2 ATPase during its mechano-chemical cycle.
R. Lewis, H. Durr, K.-P. Hopfner, and J. Michaelis (2008)
Nucleic Acids Res. 36, 1881-1890
   Abstract »    Full Text »    PDF »
Allosteric Activation of the ATPase Activity of the Escherichia coli RhlB RNA Helicase.
J. A. R. Worrall, F. S. Howe, A. R. McKay, C. V. Robinson, and B. F. Luisi (2008)
J. Biol. Chem. 283, 5567-5576
   Abstract »    Full Text »    PDF »
Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase.
B. Theissen, A. R. Karow, J. Kohler, A. Gubaev, and D. Klostermeier (2008)
PNAS 105, 548-553
   Abstract »    Full Text »    PDF »
The exon-junction-complex-component metastatic lymph node 51 functions in stress-granule assembly.
A. Baguet, S. Degot, N. Cougot, E. Bertrand, M.-P. Chenard, C. Wendling, P. Kessler, H. Le Hir, M.-C. Rio, and C. Tomasetto (2007)
J. Cell Sci. 120, 2774-2784
   Abstract »    Full Text »    PDF »
Biochemical Characterization of the ATPase and Helicase Activity of UAP56, an Essential Pre-mRNA Splicing and mRNA Export Factor.
J. Shen, L. Zhang, and R. Zhao (2007)
J. Biol. Chem. 282, 22544-22550
   Abstract »    Full Text »    PDF »
Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function.
O. Isken and L. E. Maquat (2007)
Genes & Dev. 21, 1833-3856
   Abstract »    Full Text »    PDF »
Spring-Loaded Mechanism of DNA Unwinding by Hepatitis C Virus NS3 Helicase.
S. Myong, M. M. Bruno, A. M. Pyle, and T. Ha (2007)
Science 317, 513-516
   Abstract »    Full Text »    PDF »
The abundance of RNPS1, a protein component of the exon junction complex, can determine the variability in efficiency of the Nonsense Mediated Decay pathway.
M. H. Viegas, N. H. Gehring, S. Breit, M. W. Hentze, and A. E. Kulozik (2007)
Nucleic Acids Res. 35, 4542-4551
   Abstract »    Full Text »    PDF »
Splicing remodels messenger ribonucleoprotein architecture via eIF4A3-dependent and -independent recruitment of exon junction complex components.
Z. Zhang and A. R. Krainer (2007)
PNAS 104, 11574-11579
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)