Lee Philip A, Tullman-Ercek Danielle, Georgiou George
Institute for Cellular and Molecular Biology, Department of Chemical Engineering, University of Texas, Austin, Texas 78712-0231, USA.
Annu Rev Microbiol. 2006;60:373-95. doi: 10.1146/annurev.micro.60.080805.142212.
The twin-arginine translocation (Tat) pathway is responsible for the export of folded proteins across the cytoplasmic membrane of bacteria. Substrates for the Tat pathway include redox enzymes requiring cofactor insertion in the cytoplasm, multimeric proteins that have to assemble into a complex prior to export, certain membrane proteins, and proteins whose folding is incompatible with Sec export. These proteins are involved in a diverse range of cellular activities including anaerobic metabolism, cell envelope biogenesis, metal acquisition and detoxification, and virulence. The Escherichia coli translocase consists of the TatA, TatB, and TatC proteins, but little is known about the precise sequence of events that leads to protein translocation, the energetic requirements, or the mechanism that prevents the export of misfolded proteins. Owing to the unique characteristics of the pathway, it holds promise for biotechnological applications.
双精氨酸转运(Tat)途径负责将折叠好的蛋白质转运穿过细菌的细胞质膜。Tat途径的底物包括需要在细胞质中插入辅因子的氧化还原酶、在输出前必须组装成复合物的多聚体蛋白质、某些膜蛋白以及折叠方式与Sec输出不兼容的蛋白质。这些蛋白质参与多种细胞活动,包括无氧代谢、细胞包膜生物合成、金属获取与解毒以及毒力。大肠杆菌转运体由TatA、TatB和TatC蛋白组成,但对于导致蛋白质转运的精确事件序列、能量需求或防止错误折叠蛋白质输出的机制了解甚少。由于该途径的独特特性,它在生物技术应用方面具有前景。