Related references
Note: Only part of the references are listed.Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported
Xianyue Ma et al.
EMBO JOURNAL (2010)
TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins
Carlo Maurer et al.
MOLECULAR BIOLOGY OF THE CELL (2010)
Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system
Michael J. Tarry et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Protein translocation across the bacterial cytoplasmic membrane
Arnold J. M. Driessen et al.
ANNUAL REVIEW OF BIOCHEMISTRY (2008)
Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging
Mark C. Leake et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides
Eva-Maria Strauch et al.
JOURNAL OF MOLECULAR BIOLOGY (2007)
Cysteine scanning mutagenesis and topological mapping of the Escherichia coli twin-arginine translocase TatC component
Claire Punginelli et al.
JOURNAL OF BACTERIOLOGY (2007)
The entire N-terminal half of TatC is involved in twin-arginine precursor binding
Eva Holzapfel et al.
BIOCHEMISTRY (2007)
Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component
Philip A. Lee et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Efficient twin arginine translocation (Tat) pathway transport of a precursor protein covalently anchored to its initial cpTatC binding site
F Gérard et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
C Dabney-Smith et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Targeting of unfolded PhoA to the TAT translocon of Escherichia coli
S Richter et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
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)
Characterisation of Tat protein transport complexes carrying inactivating mutations
CA McDevitt et al.
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
CML Barrett et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
Twin-arginine-specific protein export in Escherichia coli
M Müller
RESEARCH IN MICROBIOLOGY (2005)
Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
M Alami et al.
MOLECULAR CELL (2003)
Consensus structural features of purified bacterial TatABC complexes
J Oates et al.
JOURNAL OF MOLECULAR BIOLOGY (2003)
Role of the Escherichia coli Tat pathway in outer membrane integrity
B Ize et al.
MOLECULAR MICROBIOLOGY (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.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
H Mori et al.
JOURNAL OF CELL BIOLOGY (2002)
Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
G Buchanan et al.
MOLECULAR MICROBIOLOGY (2002)
Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport
H Mori et al.
FEBS LETTERS (2001)
TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
A Bolhuis et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (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)