Joshi R L, Faulhammer H, Chapeville F, Sprinzl M, Haenni A L
Institut Jacques Monod, CNRS and Université Paris VII, 2 Place Jussieu, 75251 Paris Cedex 05, France.
Nucleic Acids Res. 1984 Oct 11;12(19):7467-78. doi: 10.1093/nar/12.19.7467.
Turnip yellow mosaic virus (TYMV) Val-RNA forms a complex with the peptide elongation factor Tu (EF-Tu) in the presence of GTP: the Val-RNA is protected by EF-Tu.GTP from non-enzymatic deacylation and nuclease digestion. The determination of the length of the shortest TYMV Val-RNA fragment that binds EF-Tu.GTP leads us to conclude that the valylated aminoacyl RNA domain equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T arm is sufficient for complex formation. Since the aminoacyl RNA domain is also sufficient for adenylation by the ATP(CTP):tRNA nucleotidyltransferase, an analogy can be drawn between these two tRNA-specific proteins.
芜菁黄花叶病毒(TYMV)Val-RNA在GTP存在的情况下与肽延伸因子Tu(EF-Tu)形成复合物:Val-RNA受到EF-Tu·GTP的保护,免受非酶促脱酰基作用和核酸酶消化。对结合EF-Tu·GTP的最短TYMV Val-RNA片段长度的测定使我们得出结论,tRNA中与由受体茎和T臂形成的连续螺旋等效的氨酰化氨酰基RNA结构域足以形成复合物。由于氨酰基RNA结构域对于ATP(CTP):tRNA核苷酸转移酶的腺苷酸化也足够,因此可以在这两种tRNA特异性蛋白之间进行类比。