title: Interaction of turnip yellow mosaic virus Val-RNA with eukaryotic elongation factor EF-1 [alpha]. Search for a function.
abstract: The 3'-terminal tRNA-like structure in turnip yellow mosaic virus (TYMV) RNA can be adenylated by tRNA nucleotidyltransferase and subsequently aminoacylated by valyl-tRNA synthetase. Here we present evidence that TYMV Val-RNA can form a stable complex with eukaryotic wheat germ elongation factor EF-1alpha and GTP: the Val-RNA is protected by EF-1alpha.. GTP against digestion by RNase A. By affinity chromatography of TYMV Val-RNA fragments on immobilized EF-1alpha . GTP, it has been established that the valylated aminoacyl RNA domain, which in TYMV RNA is formed by the 3' half of the tRNA-like region, is sufficient for complex formation with EF-1alpha . GTP. The aminoacyl RNA domain is equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T stem and loop. In line with these results, the aminoacyl RNA domain in TYMV Val-RNA complexed to EF-1 alpha . GTP is resistant to digestion by RNase A. It is also shown that the TYMV RNA replicase (RNA-dependent RNA polymerase) isolated from TYMV-infected Chinese cabbage leaves does not contain tRNA nucleotidyltransferase, valyl-tRNA synthetase or EF-1alpha. This suggests that interaction of TYMV RNA with EF-1alpha is not mandatory for replicase activity.
authors.affiliation: Institut Jacques Monod, C.N.R.S. and Universite Paris VII, 2 Place Jussieu, 75251 Paris Cedex 05, France.
authors.forename: R L
authors.initials: RL
authors.lastname: Joshi
authors.forename: J M
authors.initials: JM
authors.lastname: Ravel
authors.forename: A L
authors.initials: AL
authors.lastname: Haenni
mesh_terms: D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology; D006160:Guanosine Triphosphate / Q000378:metabolism; D008969:Molecular Sequence Data; D020648:Peptide Elongation Factor 1 / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012324:RNA-Dependent RNA Polymerase / Q000378:metabolism; D013379:Substrate Specificity; D017806:Tymovirus / Q000235:genetics* / Q000502:physiology; D014637:Valine-tRNA Ligase / Q000378:metabolism
chemical_list: D020648:Peptide Elongation Factor 1; D012346:RNA, Transfer, Amino Acyl; D006160:Guanosine Triphosphate; D012324:RNA-Dependent RNA Polymerase; D014637:Valine-tRNA Ligase