Guerrier-Takada C, Altman S
Department of Biology, Yale University, New Haven, CT 06511.
Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1266-70. doi: 10.1073/pnas.89.4.1266.
Certain fragments of M1 RNA, the catalytic subunit of RNase P from Escherichia coli, either have no enzymatic activity at all or have altered substrate specificity compared with that of the intact catalytic RNA. After simple mixing in vitro, many of these fragments of M1 RNA can reassociate with other fragments to form complexes that have enzymatic activity typical of wild-type M1 RNA. Furthermore, inactive M1 RNA molecules with internal deletions can be complemented in vitro by other inactive derivatives of M1 RNA that have nonoverlapping deletions. Thus, two inactive molecules of M1 RNA can interact to form an active RNA enzyme. Functional attributes can be assigned to various regions of M1 RNA when the reconstitution process is combined with assays for activity with different substrates.
M1 RNA是来自大肠杆菌的核糖核酸酶P的催化亚基，其某些片段要么完全没有酶活性，要么与完整的催化RNA相比，底物特异性发生了改变。在体外简单混合后，许多这样的M1 RNA片段可以与其他片段重新结合形成具有野生型M1 RNA典型酶活性的复合物。此外，具有内部缺失的无活性M1 RNA分子可以在体外被其他具有非重叠缺失的M1 RNA无活性衍生物所互补。因此，两个无活性的M1 RNA分子可以相互作用形成一种活性RNA酶。当重组过程与针对不同底物的活性测定相结合时，可以将功能属性赋予M1 RNA的各个区域。
