Structure of the ribosome-bound cricket paralysis virus IRES RNA - PubMed (original) (raw)

. 2006 Dec;13(12):1092-6.

doi: 10.1038/nsmb1177. Epub 2006 Nov 19.

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• PMID: 17115051
• DOI: 10.1038/nsmb1177

Structure of the ribosome-bound cricket paralysis virus IRES RNA

Martin Schüler et al. Nat Struct Mol Biol. 2006 Dec.

Abstract

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.

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