Key result
Combined single molecule force spectroscopy and computer simulations provide a detailed understanding of how RNA-dependent RNA polymerase binding leads to extensive rearrangement of viral RNA structure.
Discusses experimental and computational approaches to understand the unfolding pathway of a viral translation enhancer.
Details viral RNA restructuring by polymerase; leaves open translation to antiviral strategies.
How plus-strand [+]RNA virus genomes transition from translation templates to replication templates is a matter of much speculation. We have previously proposed that, for Turnip crinkle virus, binding of the encoded RNA-dependent RNA polymerase (RdRp) to the 3'UTR of the [+]RNA template promotes a regional wide-spread conformational switch to an alternative structure that disassembles the cap-independent translation enhancer (CITE) in the 3'UTR. The active 3'CITE folds into a tRNA-like T-shaped structure (TSS) that binds to 80S ribosomes and 60S subunits in the P-site. In this Point-of-View, we discuss the history of our research on the TSS and our recent report combining coarse level single molecule force spectroscopy (optical tweezers) with fine-grain computer simulations of this experimental process and biochemical approaches to obtain a detailed understanding of how RdRp binding in the TSS vicinity might lead to an extensive rearrangement of the RNA structure.
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Le et al. (2017) reported a review. Combined single molecule force spectroscopy and computer simulations provide a detailed understanding of how RNA-dependent RNA polymerase binding leads to extensive rearrangement of viral RNA structure.
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