Abdurashidova G G, Ovsepian V A, Budovskiĭ E I
Mol Biol (Mosk). 1985 Jul-Aug;19(4):1148-52.
Proteins contacting (directly interacting) with peptidyl-tRNA in the A-site of E. coli ribosome were determined by means of ultraviolet-induced RNA-protein cross-linking. It has been shown that upon enzymatic binding of Phe-tRNAPhe with the posttranslocated ribosome and following transpeptidation, the peptidyl-tRNAPhe directly interacts with proteins S5, S10, L6, L16 and S13/S14/L27, while upon non-enzymatic binding--with S5, S10, L2, L6 and L16. These data evidenced, that the difference in tRNA-protein interactions upon enzymatic and non-enzymatic binding of Phe-tRNAPhe to the ribosome does not prevent the following step and remains after transpeptidation.
通过紫外线诱导的RNA-蛋白质交联法，确定了与大肠杆菌核糖体A位点的肽基-tRNA直接相互作用的蛋白质。结果表明，苯丙氨酰-tRNA苯丙氨酸与转位后的核糖体酶促结合并进行转肽作用后，肽基-tRNA苯丙氨酸与蛋白质S5、S10、L6、L16和S13/S14/L27直接相互作用，而非酶促结合时则与S5、S10、L2、L6和L16相互作用。这些数据表明，苯丙氨酰-tRNA苯丙氨酸与核糖体酶促和非酶促结合时tRNA-蛋白质相互作用的差异并不妨碍后续步骤，并且在转肽作用后仍然存在。
