Key result
A functional and structural analysis of ribosomal protein rpS25 proposes a structural model explaining its essential role in the binding of viral IRES RNAs to the 40S ribosomal subunit.
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rpS25 model refines IRES-ribosome binding insights; leaves open antiviral targeting potential.
Some viruses exploit internal initiation for their propagation in the host cell. This type of initiation is facilitated by structured elements (internal ribosome entry site, IRES) upstream of the initiator AUG and requires only a reduced number of canonical initiation factors. An important example are IRES of the virus family Dicistroviridae that bind to the inter-subunit side of the small ribosomal 40S subunit and lead to the formation of elongation-competent 80S ribosomes without the help of any initiation factor. Here, we present a comprehensive functional and structural analysis of eukaryotic-specific ribosomal protein rpS25 in the context of this type of initiation and propose a structural model explaining the essential involvement of rpS25 for hijacking the ribosome.
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Muhs et al. (2011) studied this question. A functional and structural analysis of ribosomal protein rpS25 proposes a structural model explaining its essential role in the binding of viral IRES RNAs to the 40S ribosomal subunit.
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