核糖核酸酶P RNA中的P4金属结合位点通过底物定位影响活性位点金属亲和力。
The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning.
作者信息
Christian Eric L, Smith Kari M J, Perera Nicholas, Harris Michael E
机构信息
Center for RNA Molecular Biology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
出版信息
RNA. 2006 Aug;12(8):1463-7. doi: 10.1261/rna.158606. Epub 2006 Jul 5.
Abstract
Although helix P4 in the catalytic domain of the RNase P ribozyme is known to coordinate magnesium ions important for activity, distinguishing between direct and indirect roles in catalysis has been difficult. Here, we provide evidence for an indirect role in catalysis by showing that while the universally conserved bulge of helix P4 is positioned 5 nt downstream of the cleavage site, changes in its structure can still purturb active site metal binding. Because changes in helix P4 also appear to alter its position relative to the pre-tRNA cleavage site, these data suggest that P4 contributes to catalytic metal ion binding through substrate positioning.
摘要
尽管已知核糖核酸酶P核酶催化结构域中的螺旋P4可配位对活性很重要的镁离子，但区分其在催化中的直接和间接作用一直很困难。在这里，我们通过表明虽然螺旋P4普遍保守的凸起位于切割位点下游5个核苷酸处，但其结构变化仍会扰乱活性位点金属结合，从而为其在催化中的间接作用提供了证据。由于螺旋P4的变化似乎也会改变其相对于前体tRNA切割位点的位置，这些数据表明P4通过底物定位促进催化金属离子结合。
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