Stark B C, Kole R, Bowman E J, Altman S
Proc Natl Acad Sci U S A. 1978 Aug;75(8):3717-21. doi: 10.1073/pnas.75.8.3717.
The activity of ribonuclease P on precursor tRNA substrates from Escherichia coli can be abolished by pretreatment of this enzyme with micrococcal nuclease or pancreatic ribonuclease A, as well as by proteases and by thermal denaturation. Highly purified RNase P exhibits one prominent RNA and one prominent polypeptide component when examined in polyacrylamide gels containing sodium dodecyl sulfate. The buoyant density in CsCl of RNase P, 1.71 g/ml, is characteristic of a protein-RNA complex. The activity of RNase P is inhibited by various RNA molecules. The presence of a discrete RNA component in RNase P appears to be essential for enzymatic function. A model is described for enzyme-substrate recognition in which this RNA component plays an important role.
用微球菌核酸酶、胰核糖核酸酶A对核糖核酸酶P进行预处理，以及用蛋白酶处理和热变性处理，均可消除该酶对来自大肠杆菌的前体tRNA底物的活性。在含有十二烷基硫酸钠的聚丙烯酰胺凝胶中进行检测时，高度纯化的核糖核酸酶P呈现出一个主要的RNA组分和一个主要的多肽组分。核糖核酸酶P在CsCl中的浮力密度为1.71 g/ml，这是蛋白质-RNA复合物的特征。核糖核酸酶P的活性受到各种RNA分子的抑制。核糖核酸酶P中离散RNA组分的存在似乎对酶功能至关重要。本文描述了一种酶-底物识别模型，其中该RNA组分发挥着重要作用。
