Lowary P T, Uhlenbeck O C
Department of Chemistry and Biochemistry, University of Colorado, Boulder, 80309.
Nucleic Acids Res. 1987 Dec 23;15(24):10483-93. doi: 10.1093/nar/15.24.10483.
The introduction of a cytidine in place of one of the two single stranded uridines in the R17 replicase translational operator results in a much tighter binding to R17 coat protein. The complex containing the variant RNA is stable to gel electrophoresis and has a binding constant about 50 times greater than the one with wild type RNA. The nearly thirty percent increase in the free energy of binding for the variant RNA is primarily due to a more favorable enthalpy of interaction. A possible explanation for this surprising result is that the U to C change leads to a greater extent of formation of a transient covalent complex between the protein and the RNA.
在R17复制酶翻译操纵子中,用一个胞苷取代两条单链尿苷中的一个,会导致与R17外壳蛋白的结合紧密得多。含有变异RNA的复合物对凝胶电泳稳定,其结合常数比野生型RNA的复合物大约大50倍。变异RNA结合自由能近30%的增加主要归因于更有利的相互作用焓。对这一惊人结果的一种可能解释是,U到C的变化导致蛋白质与RNA之间形成瞬时共价复合物的程度更大。