Published in J Cell Biol on April 15, 2002
The twin-arginine translocation (Tat) protein export pathway. Nat Rev Microbiol (2012) 2.53
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Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging. Proc Natl Acad Sci U S A (2008) 2.09
The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. Proc Natl Acad Sci U S A (2005) 2.02
Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition. Biochim Biophys Acta (2012) 1.34
Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway. J Bacteriol (2004) 1.34
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Structure of the TatC core of the twin-arginine protein transport system. Nature (2012) 1.23
Evidence for a dynamic and transient pathway through the TAT protein transport machinery. EMBO J (2007) 1.22
Plastid protein import and sorting: different paths to the same compartments. Curr Opin Plant Biol (2008) 1.17
Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coli. J Biol Chem (2008) 1.13
Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system. Mol Biol Cell (2009) 1.12
Mapping the signal peptide binding and oligomer contact sites of the core subunit of the pea twin arginine protein translocase. Plant Cell (2013) 1.11
Twin-arginine-dependent translocation of folded proteins. Philos Trans R Soc Lond B Biol Sci (2012) 1.09
TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli. FEBS Lett (2007) 1.06
Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation. J Biol Chem (2011) 1.05
Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported. EMBO J (2010) 1.05
TatB functions as an oligomeric binding site for folded Tat precursor proteins. Mol Biol Cell (2010) 1.04
Structural model for the protein-translocating element of the twin-arginine transport system. Proc Natl Acad Sci U S A (2013) 1.01
Mapping precursor-binding site on TatC subunit of twin arginine-specific protein translocase by site-specific photo cross-linking. J Biol Chem (2012) 1.00
Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation. J Bacteriol (2002) 0.99
Escherichia coli TatA and TatB proteins have N-out, C-in topology in intact cells. J Biol Chem (2012) 0.98
The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules. EMBO J (2008) 0.98
Structure of TatA paralog, TatE, suggests a structurally homogeneous form of Tat protein translocase that transports folded proteins of differing diameter. J Biol Chem (2011) 0.96
Stoichiometry for binding and transport by the twin arginine translocation system. J Cell Biol (2012) 0.95
Kinetics of precursor interactions with the bacterial Tat translocase detected by real-time FRET. J Biol Chem (2012) 0.92
Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system. Proc Natl Acad Sci U S A (2013) 0.91
Positive selection for loss-of-function tat mutations identifies critical residues required for TatA activity. J Bacteriol (2005) 0.91
Thylakoid targeting of Tat passenger proteins shows no delta pH dependence in vivo. EMBO J (2003) 0.91
Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells. PLoS One (2013) 0.91
The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway. Proteins (2008) 0.90
Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli. PLoS One (2012) 0.90
Subunit organization in the TatA complex of the twin arginine protein translocase: a site-directed EPR spin labeling study. J Biol Chem (2009) 0.89
Large-scale translocation reversal within the thylakoid Tat system in vivo. J Cell Biol (2005) 0.88
A little help from my friends: quality control of presecretory proteins in bacteria. J Bacteriol (2004) 0.88
Environmental salinity determines the specificity and need for Tat-dependent secretion of the YwbN protein in Bacillus subtilis. PLoS One (2011) 0.88
Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat). J Biol Chem (2015) 0.87
Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins. Proc Natl Acad Sci U S A (2012) 0.87
Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly. J Cell Biol (2014) 0.86
The chloroplast twin arginine transport (Tat) component, Tha4, undergoes conformational changes leading to Tat protein transport. J Biol Chem (2012) 0.85
Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes. Mol Microbiol (2012) 0.84
A stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane. J Biol Chem (2008) 0.82
The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli. J Biol Chem (2012) 0.82
Salt sensitivity of minimal twin arginine translocases. J Biol Chem (2011) 0.82
Formation of functional Tat translocases from heterologous components. BMC Microbiol (2006) 0.79
The TatC component of the twin-arginine protein translocase functions as an obligate oligomer. Mol Microbiol (2015) 0.79
Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts. Plant Physiol (2012) 0.79
Interaction of Mycobacterium tuberculosis Virulence Factor RipA with Chaperone MoxR1 Is Required for Transport through the TAT Secretion System. MBio (2016) 0.78
A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase. Proc Natl Acad Sci U S A (2017) 0.77
Dynamic localization of Tat protein transport machinery components in Streptomyces coelicolor. J Bacteriol (2012) 0.77
Co-factor insertion and disulfide bond requirements for twin-arginine translocase-dependent export of the Bacillus subtilis Rieske protein QcrA. J Biol Chem (2014) 0.77
A TatABC-type Tat translocase is required for unimpaired aerobic growth of Corynebacterium glutamicum ATCC13032. PLoS One (2015) 0.76
The canonical twin-arginine translocase components are not required for secretion of folded green fluorescent protein from the ancestral strain of Bacillus subtilis. Appl Environ Microbiol (2014) 0.76
The Tat substrate SufI is critical for the ability of Yersinia pseudotuberculosis to cause systemic infection. Infect Immun (2017) 0.75
TatA complexes exhibit a marked change in organisation in response to expression of the TatBC complex. Biochem J (2017) 0.75
Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase. MBio (2017) 0.75
The Tat protein export pathway. Mol Microbiol (2000) 3.89
Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature (1999) 3.78
A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase. EMBO J (1995) 2.29
Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP. J Biol Chem (1992) 2.29
Escherichia coli translocase: the unravelling of a molecular machine. Mol Microbiol (2000) 2.19
Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J Cell Biol (2001) 2.17
TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J Biol Chem (2001) 2.11
Sec-independent protein translocation by the maize Hcf106 protein. Science (1997) 2.09
Multiple pathways for protein transport into or across the thylakoid membrane. EMBO J (1993) 2.05
Chloroplast Oxa1p homolog albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes. J Biol Chem (2000) 1.77
Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. Eur J Biochem (2001) 1.55
The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane. J Biol Chem (1998) 1.47
Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways. J Cell Biol (1999) 1.41
A folded protein can be transported across the chloroplast envelope and thylakoid membranes. Mol Biol Cell (1997) 1.39
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Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways. Biochim Biophys Acta (2001) 1.32
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Dynamics of the TOM complex of mitochondria during binding and translocation of preproteins. Mol Cell Biol (1998) 1.19
Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. FEBS Lett (2001) 1.12
Chloroplast TatC plays a direct role in thylakoid (Delta)pH-dependent protein transport. FEBS Lett (2001) 1.11
The maize tha4 gene functions in sec-independent protein transport in chloroplasts and is related to hcf106, tatA, and tatB. J Cell Biol (1999) 1.09
Energy-transducing thylakoid membranes remain highly impermeable to ions during protein translocation. Proc Natl Acad Sci U S A (1998) 1.07
A signal peptide that directs non-Sec transport in bacteria also directs efficient and exclusive transport on the thylakoid Delta pH pathway. J Biol Chem (1998) 1.07
Precursors bind to specific sites on thylakoid membranes prior to transport on the delta pH protein translocation system. J Biol Chem (2000) 1.01
Molecular characterization of the Arabidopsis 9-cis epoxycarotenoid dioxygenase gene family. Plant J (2003) 3.01
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J Biol Chem (2005) 1.51
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Efficient twin arginine translocation (Tat) pathway transport of a precursor protein covalently anchored to its initial cpTatC binding site. J Biol Chem (2005) 1.23
The thylakoid proton gradient promotes an advanced stage of signal peptide binding deep within the Tat pathway receptor complex. J Biol Chem (2006) 1.17
Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system. Mol Biol Cell (2009) 1.12
Mapping the signal peptide binding and oligomer contact sites of the core subunit of the pea twin arginine protein translocase. Plant Cell (2013) 1.11
Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported. EMBO J (2010) 1.05
Functional assembly of thylakoid deltapH-dependent/Tat protein transport pathway components in vitro. Eur J Biochem (2003) 0.95
Stoichiometry for binding and transport by the twin arginine translocation system. J Cell Biol (2012) 0.95
Requirement of a Tha4-conserved transmembrane glutamate in thylakoid Tat translocase assembly revealed by biochemical complementation. J Biol Chem (2003) 0.94
Localization and integration of thylakoid protein translocase subunit cpTatC. Plant J (2009) 0.93
A petunia chorismate mutase specialized for the production of floral volatiles. Plant J (2009) 0.93
Plastids contain a second sec translocase system with essential functions. Plant Physiol (2010) 0.92
Results of a randomized crossover study comparing once-daily and thrice-daily sevelamer dosing. Am J Kidney Dis (2006) 0.88
Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly. J Cell Biol (2014) 0.86
The energetics of the chloroplast Tat protein transport pathway revisited. Trends Plant Sci (2005) 0.86
The chloroplast twin arginine transport (Tat) component, Tha4, undergoes conformational changes leading to Tat protein transport. J Biol Chem (2012) 0.85
FtsH2 and FtsH5: two homologous subunits use different integration mechanisms leading to the same thylakoid multimeric complex. Plant J (2011) 0.83