首页> 外文期刊>Nucleic Acids Research >Solution structure of human P1 center dot P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome
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Solution structure of human P1 center dot P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome

机译:人类P1中心点P2异二聚体的溶液结构为真核茎在将核糖体失活蛋白天花粉蛋白募集到核糖体中的作用提供了见解

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Lateral ribosomal stalk is responsible for binding and recruiting translation factors during protein synthesis. The eukaryotic stalk consists of one P0 protein with two copies of P1 center dot P2 heterodimers to form a P0(P1 center dot P2)(2) pentameric P-complex. Here, we have solved the structure of full-length P1 center dot P2 by nuclear magnetic resonance spectroscopy. P1 and P2 dimerize via their helical N-terminal domains, whereas the C-terminal tails of P1 center dot P2 are unstructured and can extend up to similar to 125 A away from the dimerization domains. N-15 relaxation study reveals that the C-terminal tails are flexible, having a much faster internal mobility than the N-terminal domains. Replacement of prokaryotic L10(L7/L12)(4)/L11 by eukaryotic P0(P1 center dot P2)(2)/eL12 rendered Escherichia coli ribosome, which is insensitive to trichosanthin (TCS), susceptible to depurination by TCS and the C-terminal tail was found to be responsible for this depurination. Truncation and insertion studies showed that depurination of hybrid ribosome is dependent on the length of the proline-alanine rich hinge region within the C-terminal tail. All together, we propose a model that recruitment of TCS to the sarcin-ricin loop required the flexible C-terminal tail, and the proline-alanine rich hinge region lengthens this C-terminal tail, allowing the tail to sweep around the ribosome to recruit TCS.
机译:核糖体外侧茎负责蛋白质合成过程中的结合和募集翻译因子。真核茎由一个P0蛋白和两个P1中心点P2异二聚体拷贝构成P0(P1中心点P2)(2)五聚体P-复合物。在这里,我们通过核磁共振波谱解决了全长P1中心点P2的结构。 P1和P2通过其螺旋N末端结构域进行二聚,而P1中心点P2的C末端尾巴是无结构的,并且可以从二聚结构域延伸至类似于125A。 N-15弛豫研究表明,C末端的尾巴具有柔韧性,比N末端的结构域具有更快的内部迁移率。用真核P0(P1中心点P2)(2)/ eL12取代原核L10(L7 / L12)(4)/ L11使得大肠杆菌核糖体对天花粉蛋白(TCS)不敏感,容易被TCS和C纯化-发现末端尾巴是造成这种净化的原因。截短和插入研究表明,杂合核糖体的脱嘌呤依赖于C末端尾巴中富含脯氨酸的丙氨酸铰链区的长度。总之,我们提出了一个模型,即将TCS募集到sarcin-ricin环中需要柔性C末端尾巴,脯氨酸-丙氨酸丰富的铰链区延长了该C末端尾巴,从而使尾巴围绕核糖体扫掠以募集TCS。

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