Lawrence N P, Altman S
J Mol Biol. 1986 Sep 20;191(2):163-75. doi: 10.1016/0022-2836(86)90253-6.
One addition mutation and several small deletion mutations have been created in vitro at a unique site in the gene coding for M1 RNA, the RNA subunit of Escherichia coli RNase P. The mutant genes exhibit a wide range of efficiencies in complementing another mutant that is thermosensitive for RNase P function in vivo. The transcripts of the mutated genes cleave a precursor tRNA in vitro with efficiencies that parallel their ability to function in the complementation assay in vivo. The secondary structures in solution of the mutant gene transcripts are shown to be different from the parent molecule by probing the structure of the transcripts with ribonuclease T1. A local region of secondary structure, between nucleotides 275 and 295, must be maintained for normal function of M1 RNA.
在编码大肠杆菌核糖核酸酶P的RNA亚基M1 RNA的基因的一个独特位点上，已经在体外产生了一个添加突变和几个小的缺失突变。这些突变基因在体内对核糖核酸酶P功能热敏的另一个突变体的互补中表现出广泛的效率范围。突变基因的转录本在体外切割前体tRNA的效率与其在体内互补测定中的功能能力平行。通过用核糖核酸酶T1探测转录本的结构，表明突变基因转录本在溶液中的二级结构与亲本分子不同。M1 RNA的正常功能必须维持核苷酸275至295之间二级结构的局部区域。
