Cofolding organizes alfalfa mosaic virus RNA and coat protein for replication.
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.
Guogas
Laura M
LM
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
Filman
David J
DJ
Hogle
James M
JM
Gehrke
Lee
L
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
D020413:3' Untranslated Regions; D036022:Capsid Proteins; D012367:RNA, Viral