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Originally published in Science Express on 23 November 2006
Science 1 December 2006:
Vol. 314. no. 5804, pp. 1450 - 1454
DOI: 10.1126/science.1133281
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Reports

Structural Basis for Ribosome Recruitment and Manipulation by a Viral IRES RNA

Jennifer S. Pfingsten, David A. Costantino, Jeffrey S. Kieft*

Canonical cap-dependent translation initiation requires a large number of protein factors that act in a stepwise assembly process. In contrast, internal ribosomal entry sites (IRESs) are cis-acting RNAs that in some cases completely supplant these factors by recruiting and activating the ribosome using a single structured RNA. Here we present the crystal structures of the ribosome-binding domain from a Dicistroviridae intergenic region IRES at 3.1 angstrom resolution, providing a view of the prefolded architecture of an all-RNA translation initiation apparatus. Docking of the structure into cryo–electron microscopy reconstructions of an IRES-ribosome complex suggests a model for ribosome manipulation by a dynamic IRES RNA.

Department of Biochemistry and Molecular Genetics, University of Colorado at Denver and Health Sciences Center, Mail Stop 8101, Post Office Box 6511, Aurora, CO 80045, USA.

* To whom correspondence should be addressed. E-mail: Jeffrey.Kieft{at}uchsc.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
RNA structure-based ribosome recruitment: Lessons from the Dicistroviridae intergenic region IRESes.
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Roles of the negatively charged N-terminal extension of Saccharomyces cerevisiae ribosomal protein S5 revealed by characterization of a yeast strain containing human ribosomal protein S5.
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Characterization of a cyanobacterial RNase P ribozyme recognition motif in the IRES of foot-and-mouth disease virus reveals a unique structural element.
P. Serrano, J. Gomez, and E. Martinez-Salas (2007)
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Eukaryotic ribosomal protein RPS25 interacts with the conserved loop region in a dicistroviral intergenic internal ribosome entry site.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)