The structure of helix 89 of 23S rRNA is important for peptidyl transferase function of Escherichia coli ribosome
The structure of helix 89 of 23S rRNA is important for peptidyl transferase function of Escherichia coli ribosome
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DOI：
10.1016/j.febslet.2011.08.030
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发表时间：
2011-10-03
期刊：
影响因子：
3.5
通讯作者：
Dontsova, Olga A.
中科院分区：
文献类型：
--
作者：
Burakovsky, Dmitry E.;Sergiev, Petr V.;Dontsova, Olga A.
23 SrRNA的H5 N89连接核糖体肽基转移酶中心和延伸因子结合位点。通过X射线结构分析确定的螺旋89的二级结构涉及的碱基对比相同一级结构的螺旋可绘制的碱基对少。在翻译的某个阶段，可能会出现替代性的二级结构。在此，通过定点诱变，我们稳定了“X射线”结构或具有最大数目配对核苷酸的结构。突变UU 2492 -3C是致死性的，其目的是提供23 SrRNA的螺旋89的最大配对。突变体核糖体不能独立催化肽转移与氨酰-tRNA或嘌呤霉素。(C)2011年由Elsevier B. V.代表欧洲生物化学学会联合会出版。
Helix 89 of the 23S rRNA connects ribosomal peptidyltransferase center and elongation factor binding site. Secondary structure of helix 89 determined by X-ray structural analysis involves less base pairs then could be drawn for the helix of the same primary structure. It can be that alternative secondary structure might be realized at some stage of translation. Here by means of site-directed mutagenesis we stabilized either the "X-ray" structure or the structure with largest number of paired nucleotides. Mutation UU2492-3C which aimed to provide maximal pairing of the helix 89 of the 23S rRNA was lethal. Mutant ribosomes were unable to catalyze peptide transfer independently either with aminoacyl-tRNA or puromycin. (C) 2011 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.