Bastin M, Hall T C
J Virol. 1976 Oct;20(1):117-22. doi: 10.1128/JVI.20.1.117-122.1976.
Tyrosylated Brome mosaic virus RNA was found to interact with a binary complex of wheat germ, elongation factor 1 and [3H]GTP. Increasing amounts of the aminoacylated viral RNA proportionately reduced radioactivity bound to a nitrocellulose filter, as has previously been noted by others for the charged forms of tobacco mosaic virus, turnip yellow mosaic virus, and tRNA's. However, Sephadex chromatography of the products showed that instead of forming the ternary complex elongation factor-GTP-aminoacyl RNA, the viral RNA caused release of GTP from its complex with elongation factor. Acetylated tyrosyl Brome mosaic virus RNA did not react with the binary complex,and only a slight degree, if any, of stabilization of tyrosine bound to viral RNA was observed after interaction with elongation factor 1. Although such interactions are similar to the reaction of elongation factor with aminoacyl-tRNA , the release of GTP is different and accentuates the possible role for aminoacylation in transcription rather than in translation events.
发现酪氨酰化的雀麦花叶病毒RNA与小麦胚芽、延伸因子1和[3H]GTP的二元复合物相互作用。正如其他人先前针对烟草花叶病毒、芜菁黄花叶病毒和tRNA的带电形式所指出的那样，氨基酰化病毒RNA数量的增加会相应地减少与硝酸纤维素滤膜结合的放射性。然而，对产物进行葡聚糖凝胶色谱分析表明，病毒RNA并未形成延伸因子-GTP-氨基酰RNA三元复合物，而是导致GTP从其与延伸因子的复合物中释放出来。乙酰化酪氨酰雀麦花叶病毒RNA不与该二元复合物发生反应，并且在与延伸因子1相互作用后，仅观察到与病毒RNA结合的酪氨酸有轻微程度（如果有的话）的稳定化。尽管这种相互作用类似于延伸因子与氨基酰-tRNA的反应，但GTP的释放有所不同，这突出了氨基酰化在转录而非翻译事件中的可能作用。
