The Tat pathway in bacteria and chloroplasts (Review)

被引:90
作者
Müller, M
Klösgen, RB
机构
[1] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany
[2] Univ Halle Wittenberg, Inst Plant Physiol, Halle Saale, Germany
关键词
twin-arginine; protein transport; signal sequence; thylakoid membrane; cytoplasmic membrane;
D O I
10.1080/09687860500041809
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Both in prokaryotic organisms and in chloroplasts, a specialized protein transport pathway exists which is capable of translocating proteins in a fully folded conformation. Transport is mediated in both instances by signal peptides harbouring a twin-arginine consensus motif (twin-arginine translocation ( Tat) pathway). The Tat translocase comprises the three functionally different membrane proteins TatA, TatB, and TatC. While TatB and TatC are involved in the specific recognition of the substrate, TatA might be the major pore-forming component. Current evidence suggests that a functional Tat translocase is assembled from separate TatBC and TatA assemblies only on demand, i.e., in the presence of transport substrate and a transmembrane H+-motive force.
引用
收藏
页码:113 / 121
页数:9
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