Fanning T G, Cantrell M, Shih C Y, Craven G R
Nucleic Acids Res. 1978 Mar;5(3):933-50. doi: 10.1093/nar/5.3.933.
In a previous publication1 we reported that the tyrosine selective reagent, tetraitromethane, causes complete inactivation of E. coli 30S ribosomes for poly U directed non-enzymatic phe-tRNA binding. This inactivation was demonstrated to be due to the chemical modification of the protein moiety of the ribosome. We have no identified the proteins of the 30S particle inactivated by this modification. Using a method of ribosome reconstruction we have found that unmodified proteins S1, S11, and S21 are essential for the restoration of the phe-tRNA binding activity of tetranitromethane inactivated ribosomes. We propose that these three proteins are intimately involved in the 30S ribosome binding site for tRNA.
在之前的一篇出版物1中,我们报道酪氨酸选择性试剂四硝基甲烷会导致大肠杆菌30S核糖体完全失活,从而无法进行聚U指导的非酶促苯丙氨酰-tRNA结合。这种失活被证明是由于核糖体蛋白质部分的化学修饰所致。我们尚未鉴定出因这种修饰而失活的30S颗粒中的蛋白质。通过核糖体重建方法,我们发现未修饰的蛋白质S1、S11和S21对于恢复四硝基甲烷失活核糖体的苯丙氨酰-tRNA结合活性至关重要。我们提出这三种蛋白质密切参与了30S核糖体与tRNA的结合位点。