Related references
Note: Only part of the references are listed.Structure of TatA Paralog, TatE, Suggests a Structurally Homogeneous Form of Tat Protein Translocase That Transports Folded Proteins of Differing Diameter
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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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Evidence for a dynamic and transient pathway through the TAT protein transport machinery
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Escherichia coli twin arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities
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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
C Dabney-Smith et al.
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Unassisted membrane insertion as the initial step in ΔpH/Tat-dependent protein transport
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Targeting of unfolded PhoA to the TAT translocon of Escherichia coli
S Richter et al.
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The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
Characterisation of Tat protein transport complexes carrying inactivating mutations
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BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2005)
Mutations in subunits of the Escherichia coli twin-arginine translocase block function via differing effects on translocation activity or Tat complex structure
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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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A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis
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Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
M Alami et al.
MOLECULAR CELL (2003)
Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane
N Blaudeck et al.
JOURNAL OF BACTERIOLOGY (2003)
Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport-incompetent substrate
NN Alder et al.
FEBS LETTERS (2003)
Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes
E de Leeuw et al.
JOURNAL OF MOLECULAR BIOLOGY (2002)
Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli
M Alami et al.
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A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
H Mori et al.
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Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
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Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
K Cline et al.
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TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
A Bolhuis et al.
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Functional reconstitution of bacterial Tat translocation in vitro
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