Related references
Note: Only part of the references are listed.The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding
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Tat-dependent targeting of Rieske iron-sulphur proteins to both the plasma and thylakoid membranes in the cyanobacterium Synechocystis PCC6803
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Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides
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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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The twin-arginine translocation pathway is necessary for correct membrane insertion of the Rieske Fe/S protein in Legionella pneumophila
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The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin-arginine translocase
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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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Membrane binding of twin arginine preproteins as an early step in translocation
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Targeting of unfolded PhoA to the TAT translocon of Escherichia coli
S Richter et al.
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Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea
M Dilks et al.
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Functional analysis of TatA and TatB in Streptomyces lividans
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The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter
U Gohlke et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
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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Two minimal Tat translocases in Bacillus
JDH Jongbloed et al.
MOLECULAR MICROBIOLOGY (2004)
The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway
CF Schierle et al.
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Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
M Alami et al.
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The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
TG Bernhardt et al.
MOLECULAR MICROBIOLOGY (2003)
The twin-arginine translocation (Tat) system is essential for Rhizobium-legume symbiosis
S Meloni et al.
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Role of the Escherichia coli Tat pathway in outer membrane integrity
B Ize et al.
MOLECULAR MICROBIOLOGY (2003)
Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
MP DeLisa et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2003)
Hypothesis-review - An alternative model of the twin arginine translocation system
T Bruser et al.
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Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes
E de Leeuw et al.
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Genetic analysis of the twin arginine translocator secretion pathway in bacteria
MP DeLisa 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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The Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts -: Missing link in the evolution of protein transport pathways in chloroplasts?
S Molik 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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A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif
AP Hinsley et al.
FEBS LETTERS (2001)
Functional reconstitution of bacterial Tat translocation in vitro
TL Yahr et al.
EMBO JOURNAL (2001)
Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium glutamicum respiratory chain containing an unusual diheme cytochrome c1
A Niebisch et al.
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Specificity of signal peptide recognition in Tat-dependent bacterial protein translocation
N Blaudeck et al.
JOURNAL OF BACTERIOLOGY (2001)
The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli
NR Stanley et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
Precursors bind to specific sites on thylakoid membranes prior to transport on the delta pH protein translocation system
XY Ma et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
Characterization of the early steps of OE17 precursor transport by the thylakoid ΔpH/Tat machinery
SM Musser et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2000)
The Tat protein export pathway
BC Berks et al.
MOLECULAR MICROBIOLOGY (2000)