title: The Tat pathway in bacteria and chloroplasts (review).
abstract: 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.
authors.affiliation: Institute of Biochemistry and Molecular Biology, University of Freiburg, Freiburg, Germany. matthias.mueller@biochemie.uni-freiburg.de
authors.forename: Matthias
authors.initials: M
authors.lastname: Müller
authors.forename: Ralf Bernd
authors.initials: RB
authors.lastname: Klösgen
mesh_terms: 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
chemical_list: 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