Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 33, Issue 6, Pages 274-283Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2008.04.007
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Funding
- NIAID NIH HHS [R03 AI072187, R03 AI072187-01A1, R03 AI072187-02] Funding Source: Medline
- NIGMS NIH HHS [R01 GM072560-02, R01 GM072560-04, 0805801GMC, R01 GM072560-03, R01 GM072560, R01 GM072560-01] Funding Source: Medline
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In eukaryotes, protein synthesis initiates primarily by a mechanism that requires a modified nucleotide 'cap' on the mRNA and also proteins that recruit and position the ribosome. Many pathogenic viruses use an alternative, cap-independent mechanism that substitutes RNA structure for the cap and many proteins. The RNAs driving this process are called internal ribosome-entry sites (IRESs) and some are able to bind the ribosome directly using a specific 3D RNA structure. Recent structures of IRES RNAs and IRES-ribosome complexes are revealing the structural basis of viral IRES' 'hijacking' of the protein-making machinery. It now seems that there are fundamental differences in the 3D structures used by different IRESs, although there are some common features in how they interact with ribosomes.
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