Brüser Thomas
Institute of Biology, Division of Microbiology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle, Germany.
Appl Microbiol Biotechnol. 2007 Aug;76(1):35-45. doi: 10.1007/s00253-007-0991-z. Epub 2007 May 3.
The biotechnological production of recombinant proteins is challenged by processes that decrease the yield, such as protease action, aggregation, or misfolding. Today, the variation of strains and vector systems or the modulation of inducible promoter activities is commonly used to optimize expression systems. Alternatively, aggregation to inclusion bodies may be a desired starting point for protein isolation and refolding. The discovery of the twin-arginine translocation (Tat) system for folded proteins now opens new perspectives because in most cases, the Tat machinery does not allow the passage of unfolded proteins. This feature of the Tat system can be exploited for biotechnological purposes, as expression systems may be developed that ensure a virtually complete folding of a recombinant protein before purification. This review focuses on the characteristics that make recombinant Tat systems attractive for biotechnology and discusses problems and possible solutions for an efficient translocation of folded proteins.
重组蛋白的生物技术生产面临着产量降低的问题，如蛋白酶作用、聚集或错误折叠等过程。如今，菌株和载体系统的变异或诱导型启动子活性的调节常用于优化表达系统。另外，聚集成包涵体可能是蛋白质分离和重折叠的理想起点。用于折叠蛋白的双精氨酸转运（Tat）系统的发现现在开启了新的前景，因为在大多数情况下，Tat机制不允许未折叠蛋白通过。Tat系统的这一特性可用于生物技术目的，因为可以开发出在纯化前确保重组蛋白几乎完全折叠的表达系统。本综述重点关注使重组Tat系统对生物技术具有吸引力的特性，并讨论折叠蛋白有效转运的问题及可能的解决方案。
