The Tat pathway in bacteria and chloroplasts (review).
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.
Müller
Matthias
M
Institute of Biochemistry and Molecular Biology, University of Freiburg, Freiburg, Germany. matthias.mueller@biochemie.uni-freiburg.de
Klösgen
Ralf Bernd
RB
D001426:Bacterial Proteins / Q000378:metabolism* / Q000502:physiology; D002736:Chloroplasts / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000502:physiology; D026901:Membrane Transport Proteins / Q000502:physiology*; D021382:Protein Sorting Signals / Q000502:physiology; D021381:Protein Transport; D011506:Proteins / Q000378:metabolism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D021382:Protein Sorting Signals; D011506:Proteins; C499697:TatA protein, E coli; C473116:TatB protein, E coli; C461379:TatC protein, E coli