• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Specific Inhibition of the Translocation of a Subset of Escherichia coli TAT Substrates by the TorA Signal Peptide.
【24h】

Specific Inhibition of the Translocation of a Subset of Escherichia coli TAT Substrates by the TorA Signal Peptide.

机译：TorA信号肽对大肠杆菌TAT底物亚群的特异抑制。

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

The SufI protein and the trimethylamine N-oxide reductase (TorA) are the two best-characterized prototype proteins exported by the Escherichia coli TAT system. Whereas SufI does not contain cofactors, TorA is a molybdo-enzyme and the acquisition of the molybdo-cofactor is a prerequisite for its translocation. The overproduction of each protein leads to the saturation of its translocation, but it was unknown if the overproduction of one substrate could saturate the TAT apparatus and block thus the translocation of other TAT substrates. Here, we showed that the overproduction of SufI saturated only its own translocation, but had no effect of the translocation of TorA and other TAT substrate analyzed. To dissect the saturation mechanism of TorA translocation, we shortened by about one-third of the TorA protein and removed nine consensus molybdo-cofactor-binding ligands. Like SufI, the truncated TorA (TorA502) did not contain cofactor and would not compete with the full length TorA for molybdo-cofactor acquisition. The overproduction of TorA502 completely inhibited the export of the full length TorA and dimethyl sulfoxide (DMSO) reductase, but had no effect on the translocation of SufI, nitrate-induced formate dehydrogenase and hydrogenase-2. Importantly, deletion of the twin-arginine signal peptide of TorA502 abolished the inhibitory effect. Moreover, the overproduction of the TorA signal peptide fused to the green fluorescence protein (GFP) was sufficient to block the TorA translocation. These results demonstrated that the twin-arginine signal peptide of the TorA protein specifically inhibits the translocation of a subset of TAT substrates, probably at the step of their targeting to the TAT apparatus.
机译：SufI蛋白和三甲胺N-氧化物还原酶（TorA）是大肠杆菌TAT系统输出的两个最典型的原型蛋白。 SufI不包含辅因子，而TorA是钼酶，获取钼辅因子是其易位的前提。每种蛋白质的过度生产导致其易位的饱和，但是尚不清楚一种底物的过度生产是否会使TAT装置饱和并从而阻止其他TAT底物的易位。在这里，我们表明SufI的过量生产仅饱和了其自身的易位，但对TorA和其他TAT底物的易位没有影响。为了剖析TorA易位的饱和机制，我们将TorA蛋白缩短了约三分之一，并删除了9个共有的钼-辅因子结合配体。像SufI一样，截短的TorA（TorA502）不包含辅助因子，也不会与全长TorA竞争钼辅助因子的获取。 TorA502的过量生产完全抑制了全长TorA和二甲基亚砜（DMSO）还原酶的输出，但对SufI，硝酸盐诱导的甲酸脱氢酶和加氢酶2的转运没有影响。重要的是，TorA502的双精氨酸信号肽的缺失消除了抑制作用。此外，与绿色荧光蛋白（GFP）融合的TorA信号肽的过量生产足以阻止TorA易位。这些结果表明，TorA蛋白的双精氨酸信号肽可能特异性地抑制了TAT底物的一部分的转运，可能是在它们靶向TAT装置的步骤中。

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