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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure of ERA in complex with the 3' end of 16S rRNA: Implications for ribosome biogenesis
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Structure of ERA in complex with the 3' end of 16S rRNA: Implications for ribosome biogenesis

机译：与16S rRNA 3'末端复合的ERA结构：对核糖体生物发生的影响

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摘要

ERA, composed of an N-terminal GTPase domain followed by an RNA-binding KH domain, is essential for bacterial cell viability. It binds to 16S rRNA and the 30S ribosomal subunit. However, its RNA-binding site, the functional relationship between the two domains, and its role in ribosome biogenesis remain unclear. We have determined two crystal structures of ERA, a binary complex with GDP and a ternary complex with a GTP-analog and the _(1531)AUCACCUCCUUA_(1542) sequence at the 3' end of 16S rRNA. In the ternary complex, the first nine of the 12 nucleotides are recognized by the protein. We show that GTP binding is a prerequisite for RNA recognition by ERA and that RNA recognition stimulates its GTP-hydrolyzing activity. Based on these and other data, we propose a functional cycle of ERA, suggesting that the protein serves as a chaperone for processing and maturation of 16S rRNA and a checkpoint for assembly of the 30S ribosomal subunit. The AUCA sequence is highly conserved among bacteria, archaea, and eukaryotes, whereas the CCUCC, known as the anti-Shine-Dalgamo sequence, is conserved in noneukaryotes only. Therefore, these data suggest a common mechanism for a highly conserved ERA function in all three kingdoms of life by recognizing the AUCA, with a "twist" for noneukaryotic ERA proteins by also recognizing the CCUCC.
机译：ERA由N末端GTPase结构域和RNA结合KH结构域组成，对于细菌细胞的生存能力至关重要。它与16S rRNA和30S核糖体亚基结合。然而，其RNA结合位点，两个域之间的功能关系，及其在核糖体生物发生中的作用仍不清楚。我们已经确定了ERA的两种晶体结构，即具有GDP的二元复合物和具有GTP类似物的三元复合物，以及16S rRNA的3'端的_（1531）AUCACCUCCUUA_（1542）序列。在三元复合物中，蛋白质识别出12个核苷酸中的前9个。我们表明，GTP结合是ERA识别RNA的先决条件，并且RNA识别会刺激其GTP水解活性。基于这些数据和其他数据，我们提出了ERA的功能周期，表明该蛋白可充当16S rRNA加工和成熟的分子伴侣和30S核糖体亚基装配的检查点。 AUCA序列在细菌，古细菌和真核生物中是高度保守的，而CCUCC（称为反Shine-Dalgamo序列）仅在非真核生物中是保守的。因此，这些数据表明，通过识别AUCA，可以在生命的所有三个王国中高度保守的ERA功能的共同机制，同时通过识别CCUCC，可以对真核ERA蛋白产生“扭曲”。

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  • 作者

    Chao Tu; Xiaomei Zhou; Joseph E. Tropea; Brian P. Austin; David S. Waugh; Donald L. Court; Xinhua Ji;

  • 作者单位

    Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702;

    Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702;

    Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702;

    Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702;

    Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702;

    Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702;

    Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    GTPase; KH domain; 30S ribosomal subunit;

    机译：GTP酶;KH域;30S核糖体亚基;

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