English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Structure of the ribosome-bound cricket paralysis virus IRES RNA

MPS-Authors
/persons/resource/persons50126

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

/persons/resource/persons50431

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;

/persons/resource/persons50563

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

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

Spahn.pdf
(Any fulltext), 553KB

Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-8321-7
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.