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Structure of the ribosome-bound cricket paralysis virus IRES RNA

MPG-Autoren
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Connell,  Sean R.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Mielke,  Thorsten
Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Spahn,  Christian M. T.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Zitation

Schüler, M., Connell, S. R., Lescoute, A., Giesebrecht, J., Dabrowski, M., Schroeer, B., et al. (2006). Structure of the ribosome-bound cricket paralysis virus IRES RNA. Nature Structural & Molecular Biology, 13(12), 1092-1096. doi:10.1038/nsmb1177.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0010-8321-7
Zusammenfassung
Internal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of dicistroviral IRESs can assemble elongation-competent 80S ribosomal complexes in the absence of canonical initiation factors and initiator transfer RNA. We present here a cryo-EM reconstruction of a dicistroviral IRES bound to the 80S ribosome. The resolution of the cryo-EM reconstruction, in the subnanometer range, allowed the molecular structure of the complete IRES in its active, ribosome-bound state to be solved. The structure, harboring three pseudoknot-containing domains, each with a specific functional role, shows how defined elements of the IRES emerge from a compactly folded core and interact with the key ribosomal components that form the A, P and E sites, where tRNAs normally bind. Our results exemplify the molecular strategy for recruitment of an IRES and reveal the dynamic features necessary for internal initiation.