INTERACTION OF ELONGATION-FACTOR 1 WITH AMINOACYLATED BROME MOSAIC-VIRUS AND TRANSFER-RNAS
INTERACTION OF ELONGATION-FACTOR 1 WITH AMINOACYLATED BROME MOSAIC-VIRUS AND TRANSFER-RNAS
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DOI：
10.1128/jvi.20.1.117-122.1976
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发表时间：
1976-01-01
影响因子：
5.4
通讯作者：
HALL, TC
中科院分区：
文献类型：
--
作者：
BASTIN, M;HALL, TC
酪酰化雀麦花叶病毒RNA与麦胚延伸因子1和[3 H]GTP的二元复合物相互作用增加氨酰化的病毒RNA的量会相应地减少与硝酸纤维素滤膜结合的放射性，正如其他人先前对烟草花叶病毒、芜菁黄花叶病毒和tRNA的带电形式所指出的那样。产物的Sephadex层析显示，病毒RNA没有形成延伸因子-GTP-氨酰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。乙酰化酪氨酰雀麦花叶病毒RNA不与二元复合物反应，并且在与延伸因子1相互作用后观察到与病毒RNA结合的酪氨酸的稳定化程度（如果有的话）很小。虽然这种相互作用类似于延伸因子与氨酰-tRNA的反应，但GTP的释放是不同的，并且强调了氨酰化在转录中而不是在翻译事件中的可能作用。
Tyrosylated Brome mosaic virus RNA interacted 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 was previously noted by others for the charged forms of tobacco mosaic virus, turnip yellow mosaic virus and tRNA. 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.