In a recent Nature paper, Hashem et al. attempted to probe deeper into the elusive role of eIF3 in translation initiation of viruses with hepatitis C virus-like internal ribosome entry sites (IRESs), but instead uncovered a surprising role of these IRESs in displacing eIF3 from the 40S subunit, favoring viral translation.
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Structure and function of type IV IRES in picornaviruses: a systematic review.
Front Microbiol
May 2024
College of Veterinary Medicine, Qingdao Agricultural University, Qingdao, China.
Article Synopsis
- Picornaviruses are a group of viruses with single-stranded RNA genomes, characterized by a capsid that encases their genetic material and lack an envelope.
- They contain an internal ribosome entry site (IRES), crucial for their replication and protein production, categorized into five types based on structure and function.
- Type IV IRES, known for its simpler structure similar to hepatitis C virus, is increasingly found in picornaviruses, indicating its importance in viral evolution and prompting a review of its structural and functional roles.
Structure of the RNA Specialized Translation Initiation Element that Recruits eIF3 to the 5'-UTR of c-Jun.
J Mol Biol
March 2020
Department of Chemistry, University of Washington, Seattle, WA, USA 98195. Electronic address:
Specialized translation initiation is a novel form of regulation of protein synthesis, whereby RNA structures within the 5'-UTR regulate translation rates of specific mRNAs. Similar to internal ribosome entry sites (IRESs), specialized translation initiation requires the recruitment of eukaryotic initiation factor 3 (eIF3), but also requires cap recognition by eIF3d, a new 5'-mGTP recognizing protein. How these RNA structures mediate eIF3 recruitment to affect translation of specific mRNAs remains unclear.
View Article and Find Full Text PDFUnlike for cellular mRNAs and other viral internal ribosome entry sites (IRESs), the eIF3 subunit e is not required for the translational activity of the HCV IRES.
J Biol Chem
February 2020
Univ Lyon, ENS de Lyon, Université Claude Bernard Lyon 1, CNRS UMR 5239, INSERM U1210, LBMC, 46 Allée d'Italie Site Jacques Monod, F-69007 Lyon, France. Electronic address:
Viruses depend on the host cell translation machinery for their replication, and one common strategy is the presence of internal ribosome entry sites (IRESs) in the viral RNAs, using different sets of host translation initiation factors. The hepatitis C virus (HCV) IRES binds eukaryotic translation initiation factor 3 (eIF3), but the exact functional role of the eIF3 complex and of its subunits remains to be precisely defined. Toward this goal, here we focused on eIF3 subunit e.
View Article and Find Full Text PDFHCV-like IRESs sequester eIF3: advantage virus.
Trends Microbiol
February 2014
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India. Electronic address:
In a recent Nature paper, Hashem et al. attempted to probe deeper into the elusive role of eIF3 in translation initiation of viruses with hepatitis C virus-like internal ribosome entry sites (IRESs), but instead uncovered a surprising role of these IRESs in displacing eIF3 from the 40S subunit, favoring viral translation.
View Article and Find Full Text PDFHepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunit.
Nature
November 2013
1] Howard Hughes Medical Institute (HHMI), Department of Biochemistry and Molecular Biophysics, Columbia University, New York City, New York 10032, USA [2] Department of Biochemistry and Molecular Biophysics, Columbia University, New York City, New York 10032, USA.
Hepatitis C virus (HCV) and classical swine fever virus (CSFV) messenger RNAs contain related (HCV-like) internal ribosome entry sites (IRESs) that promote 5'-end independent initiation of translation, requiring only a subset of the eukaryotic initiation factors (eIFs) needed for canonical initiation on cellular mRNAs. Initiation on HCV-like IRESs relies on their specific interaction with the 40S subunit, which places the initiation codon into the P site, where it directly base-pairs with eIF2-bound initiator methionyl transfer RNA to form a 48S initiation complex. However, all HCV-like IRESs also specifically interact with eIF3 (refs 2, 5-7, 9-12), but the role of this interaction in IRES-mediated initiation has remained unknown.
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