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硫链丝菌素与延伸因子G与核糖体蛋白L11结合结构域的相互作用。

Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain.

作者信息

Bowen William S, Van Dyke Natalya, Murgola Emanuel J, Lodmell J Stephen, Hill Walter E

机构信息

Division of Biological Sciences, The University of Montana, Missoula, Montana 59812, USA.

出版信息

J Biol Chem. 2005 Jan 28;280(4):2934-43. doi: 10.1074/jbc.M407008200. Epub 2004 Oct 18.

Abstract

Ribosomal protein L11 and the L11 binding region of ribosomal RNA constitute an important domain involved in active functions of the ribosome during translation. We studied the effects of L11 knock-out and truncation mutations on the structure of the rRNA in this region and on its interactions with a translation elongation factor and the antibiotic thiostrepton. The results indicated that the structure of the L11-binding rRNA becomes conformationally flexible when ribosomes lack the entire L11 protein, but not when the C-terminal domain is present on ribosomes. Probing wild type and mutant ribosomes in the presence of the antibiotic thiostrepton and elongation factor-G (EF-G) rigorously localized the binding cleft of thiostrepton and suggested a role for the rRNA in the L11-binding domain in modulating factor binding. Our results also provide evidence that the structure of the rRNA stabilized by the C-terminal domain of L11 is necessary to stabilize EF-G binding in the post-translocation state, and thiostrepton may modulate this structure in a manner that interferes with the ribosome-EF-G interaction. The implications for recent models of thiostrepton activity and factor interactions are discussed.

摘要

核糖体蛋白L11和核糖体RNA的L11结合区域构成了一个重要结构域,参与翻译过程中核糖体的活性功能。我们研究了L11基因敲除和截短突变对该区域rRNA结构及其与翻译延伸因子和抗生素硫链丝菌肽相互作用的影响。结果表明,当核糖体缺乏完整的L11蛋白时,L11结合rRNA的结构在构象上变得灵活,但当核糖体存在C末端结构域时则不然。在抗生素硫链丝菌肽和延伸因子G(EF-G)存在的情况下探测野生型和突变型核糖体,精确地定位了硫链丝菌肽的结合裂隙,并表明rRNA在L11结合结构域中对调节因子结合起作用。我们的结果还提供了证据,即由L11的C末端结构域稳定的rRNA结构对于在转位后状态下稳定EF-G结合是必要的,并且硫链丝菌肽可能以干扰核糖体-EF-G相互作用的方式调节这种结构。讨论了这些结果对硫链丝菌肽活性和因子相互作用的最新模型的意义。

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