Related references
Note: Only part of the references are listed.The Twin-Arginine Protein Franslocation Pathway
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Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported
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The SecY complex forms a channel capable of ionic discrimination
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The Escherichia coli Cell Division Protein and Model Tat Substrate Sufl (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like Structure
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Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides
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TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli
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Escherichia coli twin arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities
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The entire N-terminal half of TatC is involved in twin-arginine precursor binding
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The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex
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Gene splicing and mutagenesis by PCR-driven overlap extension
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Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component
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Efficient twin arginine translocation (Tat) pathway transport of a precursor protein covalently anchored to its initial cpTatC binding site
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Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
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Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
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Modeling the effects of prl mutations on the Escherichia coli SecY complex
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The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter
U Gohlke et al.
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Characterisation of Tat protein transport complexes carrying inactivating mutations
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The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex
J Oates et al.
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X-ray structure of a protein-conducting channel
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Coordinating assembly and export of complex bacterial proteins
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Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
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Role of the Escherichia coli Tat pathway in outer membrane integrity
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A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
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Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
G Buchanan et al.
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TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
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Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure
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TatD is a cytoplasmic protein with DNase activity - No requirement for TatD family proteins in Sec-independent protein export
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