| Literature DB >> 25975269 |
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.Entities:
Keywords: Signal peptide; TatA; TatC; Thylakoid membrane; Twin Arginine Translocation; chloroplast; intracellular trafficking; membrane; organelle; protein translocation
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Year: 2015 PMID: 25975269 PMCID: PMC4505407 DOI: 10.1074/jbc.R114.626820
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157