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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The Era GTPase recognizes the GAUCACCUCC sequence and binds helix 45 near the 3' end of 16S rRNA
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The Era GTPase recognizes the GAUCACCUCC sequence and binds helix 45 near the 3' end of 16S rRNA

机译：时代GTPase识别GAUCACCUCC序列并结合16S rRNA 3'末端附近的螺旋45

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摘要

Era, composed of a GTPase domain and a K homology domain, is essential for bacterial cell viability. It is required for the maturation of 16S rRNA and assembly of the 30S ribosomal subunit. We showed previously that the protein recognizes nine nucleotides (_(1531)AUCACCUCC_(1539)) near the 3 end of 16S rRNA, and that this recognition stimulates GTP-hydrolyzing activity of Era. In all three kingdoms of life, the _(1530)GAUCA_(1534) sequence and helix 45 (h45) (nucleotides 1506-1529) are highly conserved. It has been shown that the _(1530)GA_(1531) to _(1530)GA_(1531) double mutation severely affects the viability of bacteria. However, whether Era interacts with G1530 and/or h45 and whether such interactions (if any) contribute to the stimulation of Era's GTPase activity were not known. Here, we report two RNA structures that contain nucleotides 1506-1542 (RNA301), one in complex with Era and GDPNP (GNP), a nonhydro-lysable GTP-analogue, and the other in complex with Era, GNP, and the KsgA methyltransferase. The structures show that Era recognizes 10 nucleotides, including G1530, and that Era also binds h45. Moreover, GTPase assay experiments show that G1530 does not stimulate Era's GTPase activity. Rather, A1531 and A1534 are most important for stimulation and h45 further contributes to the stimulation. Although G1530 does not contribute to the intrinsic GTPase activity of Era, its interaction with Era is important for binding and is essential for the protein to function, leading to the discovery of a new cold-sensitive phenotype of Era.
机译：由GTPase结构域和K同源结构域组成的时代对于细菌细胞的生存能力至关重要。 16S rRNA的成熟和30S核糖体亚基的组装是必需的。我们以前显示该蛋白质识别16S rRNA 3末端附近的9个核苷酸（_（1531）AUCACCUCC_（1539）），并且该识别刺激了Era的GTP水解活性。在生命的所有三个王国中，_（1530）GAUCA_（1534）序列和螺旋45（h45）（核苷酸1506-1529）是高度保守的。已经显示_（1530）GA_（1531）至_（1530）GA_（1531）双重突变严重影响细菌的生存力。但是，尚不清楚Era是否与G1530和/或h45相互作用，以及此类相互作用（如果有）是否有助于刺激Era的GTPase活性。在这里，我们报告了两个包含核苷酸1506-1542（RNA301）的RNA结构，一个与Era和GDPNP（GNP）复合，一个不可水解的GTP类似物，另一个与Era，GNP和KsgA甲基转移酶复合。 。结构表明Era识别10个核苷酸，包括G1530，并且Era也结合h45。此外，GTPase分析实验表明，G1530不会刺激时代的GTPase活性。相反，A1531和A1534对刺激最为重要，而h45进一步促进了刺激。尽管G1530并不能促进Era的固有GTPase活性，但它与Era的相互作用对于结合很重要，并且对于蛋白质的功能至关重要，从而导致发现了Era的一种新的冷敏表型。

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    Chao Tu; Xiaomei Zhou; Sergey G. Tarasov; 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;

    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
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  • 关键词

    ribosome biogenesis; cell growth regulation;

    机译：核糖体生物发生;细胞生长调节;

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