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PMID: 16092529 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

The Tat pathway in bacteria and chloroplasts (review).

Molecular membrane biology ·Vol. 22 ·No. 1-2 ·2005-00-00 ·Pages 113-21

Müller M, Klösgen RB

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.

MeSH Terms
Bacterial Proteins/metabolism,physiology Chloroplasts/metabolism Escherichia coli Proteins/physiology Membrane Transport Proteins/physiology Protein Sorting Signals/physiology Protein Transport Proteins/metabolism Substrate Specificity
Chemicals
Bacterial Proteins Escherichia coli Proteins Membrane Transport Proteins Protein Sorting Signals Proteins TatA protein, E coli TatB protein, E coli TatC protein, E coli
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Müller Matthias
Institute of Biochemistry and Molecular Biology, University of Freiburg, Freiburg, Germany. matthias.mueller@biochemie.uni-freiburg.de
Klösgen Ralf Bernd
Article Info
Journal
Molecular membrane biology
Abbr.
Mol Membr Biol
ISSN
0968-7688
Published
2005-00-00
Pages
113-21
Language
English
Region
England
NLM ID
9430797
Subset
IM
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