title: Cofolding organizes alfalfa mosaic virus RNA and coat protein for replication.
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.
authors.affiliation: Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Laura M
authors.initials: LM
authors.lastname: Guogas
authors.forename: David J
authors.initials: DJ
authors.lastname: Filman
authors.forename: James M
authors.initials: JM
authors.lastname: Hogle
authors.forename: Lee
authors.initials: L
authors.lastname: Gehrke
mesh_terms: D020413:3' Untranslated Regions; D017794:Alfalfa mosaic virus / Q000737:chemistry* / Q000502:physiology*; D000595:Amino Acid Sequence; D020029:Base Pairing; D001483:Base Sequence; D001665:Binding Sites; D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012367:RNA, Viral / Q000737:chemistry* / Q000378:metabolism; D012091:Repetitive Sequences, Nucleic Acid; D014779:Virus Replication
chemical_list: D020413:3' Untranslated Regions; D036022:Capsid Proteins; D012367:RNA, Viral