Müller Matthias
Institute of Biochemistry and Molecular Biology, University of Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany.
Res Microbiol. 2005 Mar;156(2):131-6. doi: 10.1016/j.resmic.2004.09.016. Epub 2005 Jan 28.
In many prokaryotic organisms, secretory proteins harboring a twin-arginine consensus motif are exported in a fully folded conformation via the twin-arginine translocation (Tat) pathway. In Escherichia coli, Tat involves the three structurally and functionally different membrane proteins TatA, TatB, and TatC. Whereas TatC proteins function in the specific recognition of substrate, TatA might be the major pore-forming subunit.
在许多原核生物中，带有双精氨酸共有基序的分泌蛋白通过双精氨酸转运（Tat）途径以完全折叠的构象输出。在大肠杆菌中，Tat涉及三种结构和功能不同的膜蛋白TatA、TatB和TatC。虽然TatC蛋白在底物的特异性识别中起作用，但TatA可能是主要的成孔亚基。
