Key result
Subunit b of the eIF3 complex directly binds to HCV IRES domain III via its N-terminal RNA recognition motif.
Many viral mRNAs contain a 5'-UTR RNA element called internal ribosome-entry site (IRES), which bypasses the requirement of some canonical initiation factors allowing cap-independent translation. The IRES of hepatitis-C virus drives translation by directly recruiting 40S ribosomal subunits and binds to eIF3 which plays a critical role in both cap-dependent and cap-independent translation. However, the molecular basis for eIF3 activity in either case remains enigmatic. Here we report that subunit b of the eIF3 complex directly binds to HCV IRES domain III via its N-terminal-RRM. Because eIF3b was previously shown to be involved in eIF3j binding, biological implications are discussed.
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Pérard et al. (2008) studied Hepatitis C virus (HCV) translation mechanism. eIF3 subunit b was evaluated on Binding of eIF3b to HCV IRES domain III. Subunit b of the eIF3 complex directly binds to HCV IRES domain III via its N-terminal RNA recognition motif.
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