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Cofolding Organizes Alfalfa Mosaic Virus RNA and Coat Protein for Replication

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Science  17 Dec 2004:
Vol. 306, Issue 5704, pp. 2108-2111
DOI: 10.1126/science.1103399

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Abstract

Alfalfa mosaic virus genomic RNAs are infectious only when the viral coat protein binds to the RNA 3′ termini. The crystal structure of an alfalfa mosaic virus RNA-peptide complex reveals that conserved AUGC repeats and Pro-Thr-x-Arg-Ser-x-x-Tyr coat protein amino acids cofold upon interacting. Alternating AUGC residues have opposite orientation, and they base pair in different adjacent duplexes. Localized RNA backbone reversals stabilized by arginine-guanine interactions place the adenosines and guanines in reverse order in the duplex. The results suggest that a uniform, organized 3′ conformation, similar to that found on viral RNAs with transfer RNA–like ends, may be essential for replication.

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