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Mol Membr Biol. 2005 Jan-Apr;22(1-2):113-21.

The Tat pathway in bacteria and chloroplasts (review).

Author information

1
Institute of Biochemistry and Molecular Biology, University of Freiburg, Freiburg, Germany. matthias.mueller@biochemie.uni-freiburg.de

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.

PMID:
16092529
DOI:
10.1080/09687860500041809
[Indexed for MEDLINE]

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