...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >A Novel Domain in Translational GTPase BipA Mediates Interaction with the 70S Ribosome and Influences GTP Hydrolysis
【24h】

A Novel Domain in Translational GTPase BipA Mediates Interaction with the 70S Ribosome and Influences GTP Hydrolysis

机译：翻译GTPase BipA中的新域介导与70S核糖体的相互作用并影响GTP水解。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

BipA is a universally conserved prokaryotic GTPase that exhibits differential ribosome association in response to stress-related events. It is a member of the translation factor family of GTPases along with EF-G and LepA. BipA has five domains. The N-terminal region of the protein, consisting of GTPase and β-barrel domains, is common to all translational GTPases. BipA domains III and V have structural counterparts in EF-G and LepA. However, the C-terminal domain (CTD) of the protein is unique to the BipA family. To investigate how the individual domains of BipA contribute to the biological properties of the protein, deletion constructs were designed and their GTP hydrolysis and ribosome binding properties assessed. Data presented show that removal of the CTD abolishes the ability of BipA to bind to the ribosome and that ribosome complex formation requires the surface provided by domains III and V and the CTD. Additional mutational analysis was used to outline the BipA−70S interaction surface extending across these domains. Steady state kinetic analyses revealed that successive truncation of domains from the C-terminus resulted in a significant increase in the intrinsic GTP hydrolysis rate and a loss of ribosome-stimulated GTPase activity. These results indicate that, similar to other translational GTPases, the ribosome binding and GTPase activities of BipA are tightly coupled. Such intermolecular regulation likely plays a role in the differential ribosome binding by the protein
机译：BipA是一种普遍保守的原核GTP酶，在对压力相关事件的反应中显示出不同的核糖体缔合。它是GTPases和EF-G和LepA的翻译因子家族的成员。 BipA具有五个域。蛋白质的N端区域由GTPase和β-barrel结构域组成，对所有翻译GTPases都是共有的。 BipA结构域III和V在EF-G和LepA中具有结构对应物。但是，该蛋白的C末端结构域（CTD）对于BipA家族而言是唯一的。为了研究BipA的各个结构域如何促进蛋白质的生物学特性，设计了缺失构建体，并评估了其GTP水解和核糖体结合特性。呈现的数据表明，去除CTD消除了BipA与核糖体结合的能力，而核糖体复合物的形成需要结构域III和V以及CTD提供的表面。额外的突变分析被用来勾勒跨越这些域的BipA-70S相互作用表面。稳态动力学分析表明，从C端开始连续截短结构域会导致内在GTP水解速率显着增加，并失去核糖体刺激的GTPase活性。这些结果表明，与其他翻译GTP酶类似，BipA的核糖体结合和GTPase活性紧密相关。这种分子间调节可能在蛋白质与核糖体的差异结合中起作用

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号