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首页> 外文期刊>Biochemistry >Specific interactions of the L10(L12)(4) ribosomal protein complex with mRNA, rRNA, and L11
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Specific interactions of the L10(L12)(4) ribosomal protein complex with mRNA, rRNA, and L11

机译：L10（L12）（4）核糖体蛋白复合物与mRNA，rRNA和L11的特异性相互作用

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摘要

Large ribosomal subunit proteins L10 and L12 forma pentameric protein complex, L10(L12)(4), that is intimately involved in the ribosome elongation cycle. Its contacts with rRNA or other ribosomal proteins have been only partially resolved by crystallography. In Escherichia coli, L10 and L 12 are encoded from a single operon for which L10(L 12)(4) is a translational repressor that recognizes a secondary structure in the mRNA leader. In this study, L10(L12)(4) was expressed from the moderate thermophile Bacillus stearothermophilus to quantitatively compare strategies for binding of the complex to mRNA and ribosome targets. The minimal mRNA recognition structure is widely distributed among bacteria and has the potential to form a kink-turn structure similar to one identified in the rRNA as part of the L10(L12)(4) binding site. Mutations in equivalent positions between the two sequences have similar effects on L10(L12)(4)-RNA binding affinity and identify the kink-turn motif and a loop AA sequence as important recognition elements. In contrast to the larger rRNA structure, the mRNA apparently positions the kink-turn motif and loop for protein recognition without the benefit of Mg2+-dependent tertiary structure. The mRNA and rRNA fragments bind L10(L12)(4) with similar affinity (similar to 10(8) M-1), but fluorescence binding studies show that a nearby protein in the ribosome, L11, enhances L10(L12)(4) binding similar to 100-fold. Thus, mRNA and ribosome targets use similar RNA features, held in different structural contexts, to recognize L10(L12)(4), and the ribosome ensures the saturation of its L10(L12)(4) binding site by means of an additional protein-protein interaction.
机译：大型核糖体亚基蛋白L10和L12形成五聚体蛋白复合物L10（L12）（4），与核糖体延长周期密切相关。它与rRNA或其他核糖体蛋白的接触仅通过晶体学已部分解决。在大肠杆菌中，L10和L 12是从单个操纵子编码的，L10（L 12）（4）是单个操纵子，是识别mRNA前导序列中二级结构的翻译阻遏物。在这项研究中，L10（L12）（4）从嗜热嗜热脂肪芽孢杆菌中表达，以定量比较复合物与mRNA和核糖体靶标的结合策略。最小的mRNA识别结构广泛分布于细菌之间，并有可能形成扭折转弯结构，类似于在rRNA中作为L10（L12）（4）结合位点的一部分所识别的结构。两个序列之间等效位置的突变对L10（L12）（4）-RNA结合亲和力具有相似的影响，并将扭结转基序和AA环序列识别为重要的识别元件。与较大的rRNA结构相比，mRNA显然可以定位扭结转折基序和环以进行蛋白质识别，而无需使用Mg2 +依赖的三级结构。 mRNA和rRNA片段以相似的亲和力（类似于10（8）M-1）结合L10（L12）（4），但是荧光结合研究表明，核糖体中的附近蛋白质L11增强了L10（L12）（4） ）绑定类似100倍。因此，mRNA和核糖体靶标使用相似的RNA特征（在不同的结构上下文中保留）来识别L10（L12）（4），并且核糖体通过其他蛋白质确保其L10（L12）（4）结合位点饱和-蛋白质相互作用。

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