The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA
Abstract
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.
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Cites
The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
Le Hir, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.24.6860 · Cited by 971
The DEAD-box protein family of RNA helicases
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Structural Basis for RNA Unwinding by the DEAD-Box Protein Drosophila Vasa
Sengoku, T., Nureki, O., Nakamura, A., Kobayashi, S., & Yokoyama, S. (2006) · Cell · doi:10.1016/j.cell.2006.01.054 · Cited by 573
Nonsense-mediated mRNA decay: molecular insights and mechanistic variations across species
Conti, E., & Izaurralde, E. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.04.005 · Cited by 479
Mechanistic links between nonsense-mediated mRNA decay and pre-mRNA splicing in mammalian cells
Lejeune, F., & Maquat, L. E. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.03.002 · Cited by 430
The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity
Ballut, L., Marchadier, B., Baguet, A., Tomasetto, C., Séraphin, B., & Le Hir, H. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb990 · Cited by 358
Self-citationGehring, N. H., Kunz, J. B., Neu-Yilik, G., Breit, S., Viegas, M. H., Hentze, M. W., & Kulozik, A. E. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.012 · Cited by 329
Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase
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Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
Caruthers, J. M., Johnson, E. R., & McKay, D. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.24.13080 · Cited by 292
Y14 and hUpf3b Form an NMD-Activating Complex
Gehring, N. H., Neu-Yilik, G., Schell, T., Hentze, M. W., & Kulozik, A. E. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00142-4 · Cited by 291
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RNA‐binding proteins and post‐transcriptional gene regulation
Glisovic, T., Bachorik, J. L., Yong, J., & Dreyfuss, G. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.004 · Cited by 1,398
NMD: a multifaceted response to premature translational termination
Kervestin, S., & Jacobson, A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3454 · Cited by 572
Mechanism and regulation of the nonsense-mediated decay pathway
Hug, N., Longman, D., & Cáceres, J. F. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw010 · Cited by 535
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Metadata
- Authors
- Andersen, C. B. F., Ballut, L., Johansen, J. S., Chamieh, H., Nielsen, K. H., Oliveira, C. L. P., Pedersen, J. S., Séraphin, B., Hir, H. L., & Andersen, G. R.
- Venue
- Science
- Published
- 2006-09-29
- Volume
- 313
- Issue
- 5795
- Pages
- 1968-1972
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2035595761
- Cited by
- 438
- References
- 27
- FWCI
- 11.30
- Type
- journal article
- Language
- en
- Open access
- closed
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- Andersen, C. B. F., Ballut, L., Johansen, J. S., Chamieh, H., Nielsen, K. H., Oliveira, C. L. P., Pedersen, J. S., Séraphin, B., Hir, H. L., & Andersen, G. R. (2006). Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA. Science. https://doi.org/10.1126/science.1131981
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