Hayes F, Vasseur M
Eur J Biochem. 1976 Jan 15;61(2):433-42. doi: 10.1111/j.1432-1033.1976.tb10037.x.
An RNase activity probably involved in the maturation of 16-S pre-ribosomal RNA in Escherichia coli has been partially purified from crude cell extracts. When 27-S ribosome precursor particles are incubated with this enzyme preparation in vitro, their 17-S RNA is converted to a product with the same electrophoretic mobility as mature 16-S rRNA. Fingerprint analysis of this product shows that it contains the 3'-OH but not the 5'-P terminus of mature 16-S rRNA. Generation of the normal 5'-P terminus seems to require a factor present in cell extracts since incubation of the 27-S precursor particle in an extract obtained after centrifugation at 30 000 x g causes conversion of the 17-S RNA to a 16-S species containing both termini of mature 16-S rRNA. Preliminary experiments suggest that correct maturation of the 5' end of the 17-S precursor RNA requires a system in which protein synthesis can take place.
一种可能参与大肠杆菌16-S前核糖体RNA成熟过程的核糖核酸酶活性已从粗细胞提取物中得到部分纯化。当27-S核糖体前体颗粒在体外与这种酶制剂一起温育时，其17-S RNA会转化为一种电泳迁移率与成熟16-S rRNA相同的产物。对该产物的指纹分析表明，它含有成熟16-S rRNA的3'-OH末端，但不含有5'-P末端。正常5'-P末端的产生似乎需要细胞提取物中存在的一种因子，因为将27-S前体颗粒在30000×g离心后得到的提取物中温育，会使17-S RNA转化为一种含有成熟16-S rRNA两个末端的16-S产物。初步实验表明，17-S前体RNA 5'端的正确成熟需要一个能够进行蛋白质合成的系统。
