Krauss G, Peters F, Maass G
Nucleic Acids Res. 1976 Mar;3(3):631-9. doi: 10.1093/nar/3.3.631.
The interaction between tRNAPhe (yeast), from which the Y-base has been removed by acid treatment, and phenylalanyl-tRNA synthetase (yeast) has been investigated by fluorescence competition titrations and sedimentation velocity runs. The binding parameters are given under various ionic conditions. The tRNAPhe-Y still can occupy the specific binding sites on the enzyme. Compared to unmodified tRNAPhe, the binding constant is lowered by more than one order of magnitude. It can be concluded that the Y-base is not necessary for specific recognition of tRNAPhe by the cognate synthetase, it rather may represent a point of attachment for the synthetase.
通过荧光竞争滴定和沉降速度实验,研究了经酸处理去除Y碱基的酵母苯丙氨酸转运核糖核酸(tRNAPhe)与酵母苯丙氨酰 - tRNA合成酶之间的相互作用。给出了不同离子条件下的结合参数。tRNAPhe - Y仍可占据酶上的特定结合位点。与未修饰的tRNAPhe相比,结合常数降低了一个多数量级。可以得出结论,Y碱基对于同源合成酶特异性识别tRNAPhe并非必需,它更可能是合成酶的一个附着点。