Aminoacylation identity switch of turnip yellow mosaic virus RNA from valine to methionine results in an infectious virus.
The turnip yellow mosaic virus genomic RNA terminates at its 3' end in a tRNA-like structure that is capable of specific valylation. By directed mutation, the aminoacylation specificity has been switched from valine to methionine, a novel specificity for viral tRNA-like structures. The switch to methionine specificity, assayed in vitro under physiological buffer conditions with wheat germ methionyl-tRNA synthetase, required mutation of the anticodon loop and the acceptor stem pseudoknot. The resultant methionylatable genomes are infectious and stable in plants, but genomes that lack strong methionine acceptance (as previously shown with regard to valine acceptance) replicate poorly. The results indicate that amplification of turnip yellow mosaic virus RNA requires aminoacylation, but that neither the natural (valine) specificity nor interaction specifically with valyl-tRNA synthetase is crucial.
Department of Agricultural Chemistry, Oregon State University, Corvallis 97331-7301, USA.
T W
TW
Dreher
C H
CH
Tsai
J M
JM
Skuzeski
D007700:Kinetics; D008715:Methionine; D008718:Methionine-tRNA Ligase / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D009690:Nucleic Acid Conformation; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry*; D012367:RNA, Viral / Q000737:chemistry*; D013329:Structure-Activity Relationship; D017806:Tymovirus / Q000235:genetics* / Q000472:pathogenicity; D014633:Valine; D014771:Virion / Q000737:chemistry
D012346:RNA, Transfer, Amino Acyl; D012367:RNA, Viral; D008715:Methionine; D008718:Methionine-tRNA Ligase; D014633:Valine