Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; email:
Annu Rev Biochem. 2015;84:843-64. doi: 10.1146/annurev-biochem-060614-034251. Epub 2014 Dec 8.
The twin-arginine translocation (Tat) system, found in prokaryotes, chloroplasts, and some mitochondria, allows folded proteins to be moved across membranes. How this transport is achieved without significant ion leakage is an intriguing mechanistic question. Tat transport is mediated by complexes formed from small integral membrane proteins from just two protein families. Atomic-resolution structures have recently been determined for representatives of both these protein families, providing the first molecular-level glimpse of the Tat machinery. I review our current understanding of the mechanism of Tat transport in light of these new structural data.
双精氨酸转运(Tat)系统存在于原核生物、叶绿体和一些线粒体中,允许折叠蛋白跨膜运输。这种运输是如何在没有明显离子泄漏的情况下实现的,这是一个有趣的机械问题。Tat 运输是由来自两个蛋白质家族的小整合膜蛋白形成的复合物介导的。最近,这两个蛋白质家族的代表都确定了原子分辨率的结构,为 Tat 机械提供了第一个分子水平的观察。我根据这些新的结构数据回顾了我们对 Tat 运输机制的现有理解。