• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Structural Basis for Translation Termination on a Pseudouridylated Stop Codon
【24h】

Structural Basis for Translation Termination on a Pseudouridylated Stop Codon

机译：伪尿酰化终止密码子翻译终止的结构基础

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

Pseudouridylation of messenger RNA emerges as an abundant modification involved in gene expression regulation. Pseudouridylation of stop codons in eukaryotic and bacterial cells results in stop-codon read through. The structural mechanism of this phenomenon is not known. Here we present a 3.1-angstrom crystal structure of Escherichia coli release factor 1 (RF1) bound to the 70S ribosome in response to the Psi AA codon. The structure reveals that recognition of a modified stop codon does not differ from that of a canonical stop codon. Our in vitro biochemical results support this finding by yielding nearly identical rates for peptide release from E. coli ribosomes programmed with pseudouridylated and canonical stop codons. The crystal structure also brings insight into E. coli RF1-specific interactions and suggests involvement of L27 in bacterial translation termination. Our results are consistent with a mechanism in which read through of a pseudouridylated stop codon in bacteria results from increased decoding by near-cognate tRNAs (miscoding) rather than from decreased efficiency of termination. (c) 2016 Published by Elsevier Ltd.
机译：信使RNA的伪尿苷化作用是涉及基因表达调控的大量修饰。真核细胞和细菌细胞中终止密码子的伪尿苷酸化导致终止密码子通读。这种现象的结构机理尚不清楚。在这里，我们介绍了响应于Psi AA密码子结合到70S核糖体的大肠杆菌释放因子1（RF1）的3.1埃晶体结构。该结构表明，修饰终止密码子的识别与规范终止密码子的识别没有区别。我们的体外生化结果通过从伪核糖化和规范终止密码子编程的大肠杆菌核糖体中释放出几乎相同的肽释放速率，为这一发现提供了支持。晶体结构还可以深入了解大肠杆菌RF1特异性相互作用，并暗示L27参与细菌翻译终止。我们的结果与一种机制一致，在这种机制中，细菌中伪尿苷酸化终止密码子的通读是由于近同源tRNA的解码增加（误编码）而不是终止效率降低所致。 （c）2016由爱思唯尔有限公司出版。

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