• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of structural and functional genomics >Enhanced Expression and Purification of Membrane Proteins by SUMO Fusion in Escherichia coli
【24h】

Enhanced Expression and Purification of Membrane Proteins by SUMO Fusion in Escherichia coli

机译：SUMO融合蛋白在大肠杆菌中增强的膜蛋白表达和纯化

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Severe acute respiratory syndrome coronavirus (SARS-CoV) membrane protein and 5-lipoxygenase-activating protein (FLAP) are among a large number of membrane proteins that are poorly expressed when traditional expression systems and methods are employed. Therefore to efficiently express difficult membrane proteins, molecular biologists will have to develop novel or innovative expression systems. To this end, we have expressed the SARS-CoV M and FLAP proteins in Escherichia coli by utilizing a novel gene fusion expression system that takes advantage of the natural chaperoning properties of the SUMO (small ubiquitin-related modifier) tag. These chaperoning properties facilitate proper protein folding, which enhances the solubility and biological activity of the purified protein. In addition to these advantages, we found that SUMO Protease 1, can cleave the SUMO fusion high specificity to generate native protein. Herein, we demonstrate that the expression of FLAP and SARS-CoV membrane proteins are greatly enhanced by SUMO fusions in E. coli.
机译：严重的急性呼吸系统综合症冠状病毒（SARS-CoV）膜蛋白和5-脂氧合酶激活蛋白（FLAP）是大量膜蛋白中的一种，这些蛋白在采用传统表达系统和方法时表达不佳。因此，为了有效表达困难的膜蛋白，分子生物学家将不得不开发新颖或创新的表达系统。为此，我们已经利用新型的基因融合表达系统在大肠杆菌中表达了SARS-CoV M和FLAP蛋白，该系统利用了SUMO（小泛素相关修饰物）标签的天然伴侣特性。这些分子伴侣特性有助于适当的蛋白质折叠，从而增强了纯化蛋白质的溶解度和生物活性。除了这些优点外，我们发现SUMO蛋白酶1可以以高特异性切割SUMO融合蛋白以生成天然蛋白。在这里，我们证明了SUMO融合在大肠杆菌中大大提高了FLAP和SARS-CoV膜蛋白的表达。

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