title: Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).
abstract: The twin arginine translocase (Tat) transports folded proteins of widely varying size across ionically tight membranes with only 2-3 components of machinery and the proton motive force. Tat operates by a cycle in which the receptor complex combines with the pore-forming component to assemble a new translocase for each substrate. Recent data on component and substrate organization in the receptor complex and on the structure of the pore complex inform models for translocase assembly and translocation. A translocation mechanism involving local transient bilayer rupture is discussed.
authors.affiliation: From the Plant Molecular and Cellular Biology, University of Florida, Gainesville, Florida 32611 kcline@ufl.edu.
authors.forename: Kenneth
authors.initials: K
authors.lastname: Cline
mesh_terms: D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism*; D017510:Protein Folding; D021382:Protein Sorting Signals; D021381:Protein Transport
chemical_list: D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D021382:Protein Sorting Signals; C408585:twin-arginine translocase complex, E coli
keywords: Signal peptide; TatA; TatC; Thylakoid membrane; Twin Arginine Translocation; chloroplast; intracellular trafficking; membrane; organelle; protein translocation