title: Viral IRES RNA structures and ribosome interactions.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Genetics, University of Colorado Denver School of Medicine, Mail stop 8101, PO Box 6511, Aurora, CO 80045, USA. Jeffrey.kieff@uchsc.edu
authors.forename: Jeffrey S
authors.initials: JS
authors.lastname: Kieft
mesh_terms: D009690:Nucleic Acid Conformation; D012315:RNA Caps / Q000737:chemistry / Q000378:metabolism*; D012367:RNA, Viral / Q000737:chemistry / Q000378:metabolism*; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism*; D014780:Viruses / Q000378:metabolism*
chemical_list: D012315:RNA Caps; D012367:RNA, Viral