title: Translation of a nonpolyadenylated viral RNA is enhanced by binding of viral coat protein or polyadenylation of the RNA.
abstract: On entering a host cell, positive-strand RNA virus genomes have to serve as messenger for the translation of viral proteins. Efficient translation of cellular messengers requires interactions between initiation factors bound to the 5'-cap structure and the poly(A) binding protein bound to the 3'-poly(A) tail. Initiation of infection with the tripartite RNA genomes of alfalfa mosaic virus (AMV) and viruses from the genus Ilarvirus requires binding of a few molecules of coat protein (CP) to the 3' end of the nonpolyadenylated viral RNAs. Moreover, infection with the genomic RNAs can be initiated by addition of the subgenomic messenger for CP, RNA 4. We report here that extension of the AMV RNAs with a poly(A) tail of 40 to 80 A-residues permitted initiation of infection independently of CP or RNA 4 in the inoculum. Specifically, polyadenylation of RNA 1 relieved an apparent bottleneck in the translation of the viral RNAs. Translation of RNA 4 in plant protoplasts was autocatalytically stimulated by its encoded CP. Mutations that interfered with CP binding to the 3' end of viral RNAs reduced translation of RNA 4 to undetectable levels. Possibly, CP of AMV and ilarviruses stimulates translation of viral RNAs by acting as a functional analogue of poly(A) binding protein or other cellular proteins.
authors.affiliation: Institute of Molecular Plant Sciences, Gorlaeus Laboratories, Leiden University, PO Box 9502, 2300 RA, Leiden, The Netherlands.
authors.forename: L
authors.initials: L
authors.lastname: Neeleman
authors.forename: R C
authors.initials: RC
authors.lastname: Olsthoorn
authors.forename: H J
authors.initials: HJ
authors.lastname: Linthorst
authors.forename: J F
authors.initials: JF
authors.lastname: Bol
mesh_terms: D017794:Alfalfa mosaic virus / Q000235:genetics / Q000472:pathogenicity / Q000502:physiology; D019177:Bromoviridae / Q000235:genetics / Q000472:pathogenicity / Q000502:physiology; D002213:Capsid / Q000378:metabolism*; D036022:Capsid Proteins; D011485:Protein Binding; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D014026:Nicotiana / Q000821:virology; D014779:Virus Replication
chemical_list: D036022:Capsid Proteins; D012333:RNA, Messenger; D012367:RNA, Viral; C095691:coat protein, Alfalfa mosaic virus