Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Annu Rev Genet. 2012;46:209-31. doi: 10.1146/annurev-genet-110711-155427. Epub 2012 Aug 28.
Colicins are protein toxins produced by Escherichia coli to kill related bacteria. They must cross the target cell outer membrane (OM), and some must also cross the inner membrane (IM). To accomplish cellular import, colicins have parasitized E. coli nutrient transporters as well as IM and periplasmic proteins normally used to maintain cell wall integrity or provide energy for nutrient uptake through transporters. Colicins have evolved to use both transporters and other membrane proteins through mechanisms different from those employed in physiological substrate uptake. Extended receptor-binding domains allow some colicins to search by lateral diffusion for binding sites on their OM translocators while bound to their primary OM receptor. Transport across the OM is initiated by entry of the unstructured N-terminal translocation domain into the translocator. Periplasmic and IM networks subsequently accomplish insertion of the colicin cytotoxic domain into or across the IM.
肠毒素是由大肠杆菌产生的蛋白质毒素,用于杀死相关细菌。它们必须穿过靶细胞的外膜(OM),有些还必须穿过内膜(IM)。为了完成细胞内导入,肠毒素已经寄生了大肠杆菌的营养转运蛋白以及通常用于维持细胞壁完整性或通过转运蛋白为营养摄取提供能量的内膜和周质蛋白。肠毒素通过与生理底物摄取不同的机制进化为利用转运蛋白和其他膜蛋白。扩展的受体结合结构域使一些肠毒素能够在与主要 OM 受体结合的同时通过侧向扩散搜索其 OM 转运器上的结合位点。OM 的转运是通过未折叠的 N 端转运结构域进入转运器而开始的。随后,周质和 IM 网络完成将肠毒素细胞毒性结构域插入或穿过 IM。