Pieler T, Erdmann V A
Proc Natl Acad Sci U S A. 1982 Aug;79(15):4599-603. doi: 10.1073/pnas.79.15.4599.
Escherichia coli 5S RNA and its specific protein complexes were hydrolyzed with the single-strand-specific nuclease S1. Based on the results, a tertiary structural model for E. coli 5S RNA is proposed in which ribosomal proteins E-L5, E-L18, and E-L25 influence the conformation of the RNA. This may be of significance for ribosomal function. Comparison of the proposed E. coli 5S RNA structure with those of 18 other prokaryotic 5S RNAs led to a generalized eubacterial 5S RNA tertiary structure in which the majority of the conserved nucleotides are in non-base-paired regions and several conserved "looped-out" adenines (in E. coli, adenines -52, -53, -57, -58, and -66) are implied to be important for protein recognition or interaction or both.
用单链特异性核酸酶S1水解大肠杆菌5S RNA及其特异性蛋白质复合物。基于这些结果，提出了大肠杆菌5S RNA的三级结构模型，其中核糖体蛋白E-L5、E-L18和E-L25影响RNA的构象。这可能对核糖体功能具有重要意义。将所提出的大肠杆菌5S RNA结构与其他18种原核生物5S RNA的结构进行比较，得出了一个广义的真细菌5S RNA三级结构，其中大多数保守核苷酸位于非碱基配对区域，并且几个保守的“环出”腺嘌呤（在大肠杆菌中，腺嘌呤-52、-53、-57、-58和-66）被认为对蛋白质识别或相互作用或两者都很重要。
