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ReportsCofolding Organizes Alfalfa Mosaic Virus RNA and Coat Protein for ReplicationAlfalfa 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 RNAlike ends, may be essential for replication.
1 Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA. * To whom correspondence should be addressed. E-mail: Lee_Gehrke{at}hms.harvard.edu (L.G.); James_Hogle{at}hms.harvard.edu (J.M.H.)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)