tRNA binding modifies the properties of the small ribosomal subunit of rat liver.
tRNA binding modifies the properties of the small ribosomal subunit of rat liver.
复制标题
tRNA 结合改变了大鼠肝脏小核糖体亚基的特性。
作者：
A. Reboud;S. Dubost;J. Reboud
在适当的密码子存在下，特定的tRNA（酰化或未酰化）与40 S亚基的结合显示出对亚基产生两种显著的影响。首先，亚基不再能够在低离子强度下二聚化。第二，他们成为完全耐1.25 M氯化锂处理：结合tRNA防止亚基失活测量聚苯丙氨酸合成，它也防止大沉降变化的亚基和核糖体蛋白质释放氯化锂诱导。受保护的蛋白质的数量远远超过在254 nm照射后与tRNA交联的蛋白质的数量（A. M. REBOUD，S.杜博斯特和J. P.雷博德（1983）FEBS Lett. 158，285-288）。这些结果强烈表明，tRNA结合诱导的rRNA-蛋白质相互作用的亚基的大域的修改。tRNA与40 S亚基的弱相互作用被证明在密码子的情况下。
The binding of a specific tRNA (acylated or not) to the 40S subunits in the presence of the proper codon was shown to produce two striking effects on the subunits. First, the subunits were no longer able to dimerize at low ionic strength. Second, they became fully resistant to 1.25 M LiCl treatment: bound tRNA prevented subunit inactivation as measured by polyphenylalanine synthesis; it also prevented large sedimentation changes of subunits and ribosomal protein release induced by LiCl. The number of protected proteins far exceeded that of the proteins crosslinked with tRNA after irradiation at 254 nm (A.M. REBOUD, S. DUBOST and J.P. REBOUD (1983) FEBS Lett. 158, 285-288). These results strongly suggest that tRNA binding induces modifications of rRNA-protein interactions in large domains of the subunits. A weak interaction of tRNA with the 40S subunit was demonstrated in the absence of the codon.