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Volumn 10, Issue 7, 2012, Pages 483-496

The twin-arginine translocation (Tat) protein export pathway

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MEMBRANE COFACTOR PROTEIN; METAL ION; PROTEIN; TATA PROTEIN; TATB PROTEIN; TATBC PROTEIN; TATC PROTEIN; TWIN ARGININE TRANSLOCATION PROTEIN; UNCLASSIFIED DRUG;

EID: 84862501228     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro2814     Document Type: Review
Times cited : (400)

References (147)
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    • A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase
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    • Hatzixanthis, K., Palmer, T. & Sargent, F. A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. Mol. Microbiol. 49, 1377-1390 (2003). This study shows that the bacterial Tat pathway assembles substrate proteins containing TMHs.
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    • Functional Tat transport of unstructured, small, hydrophilic proteins
    • References 58 and 58 demonstrate that some small, unfolded proteins can be transported through the Tat system in plants and bacteria
    • Richter, S., Lindenstrauss, U., Lucke, C., Bayliss, R. & Bruser, T. Functional Tat transport of unstructured, small, hydrophilic proteins. J. Biol. Chem. 282, 33257-33264 (2007). References 58 and 58 demonstrate that some small, unfolded proteins can be transported through the Tat system in plants and bacteria.
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    • Functional reconstitution of bacterial Tat translocation in vitro
    • This report describes the development of an in vitro system for the analysis of the E. coli Tat transport pathway and demonstrates that ATP is not required for Tat-mediated transport
    • Yahr, T. L. & Wickner, W. T. Functional reconstitution of bacterial Tat translocation in vitro. EMBO J. 20, 2472-2479 (2001). This report describes the development of an in vitro system for the analysis of the E. coli Tat transport pathway and demonstrates that ATP is not required for Tat-mediated transport.
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    • Yahr, T.L.1    Wickner, W.T.2
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    • Energetics of protein transport across biological membranes. A study of the thylakoid ΔpH-dependent/cpTat pathway
    • This is the most detailed study on the energetics associated with protein transport by the Tat pathway
    • Alder, N. N. & Theg, S. M. Energetics of protein transport across biological membranes. a study of the thylakoid ΔpH-dependent/cpTat pathway. Cell 112, 231-242 (2003). This is the most detailed study on the energetics associated with protein transport by the Tat pathway.
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    • Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport
    • Mori, H., Summer, E. J. & Cline, K. Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport. FEBS Lett. 501, 65-68 (2001).
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    • Localization and integration of thylakoid protein translocase subunit cpTatC
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    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • This is the first article to report the purification of the TatBC complex and to show that TatB and TatC are present at equal stoichiometry in the complex
    • Bolhuis, A., Mathers, J. E., Thomas, J. D., Barrett, C. M. & Robinson, C. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 276, 20213-20219 (2001). This is the first article to report the purification of the TatBC complex and to show that TatB and TatC are present at equal stoichiometry in the complex.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20213-20219
    • Bolhuis, A.1    Mathers, J.E.2    Thomas, J.D.3    Barrett, C.M.4    Robinson, C.5
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    • Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system
    • This investigation yields the first low-resolution structures of purified TatBC with bound substrates
    • Tarry, M. J. et al. Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system. Proc. Natl Acad. Sci. USA 106, 13284-13289 (2009). This investigation yields the first low-resolution structures of purified TatBC with bound substrates.
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    • Tarry, M.J.1
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    • TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli
    • Orriss, G. L. et al. TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli. FEBS Lett. 581, 4091-4097 (2007).
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    • Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase
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    • (2011) J. Mol. Microbiol. Biotechnol. , vol.20 , pp. 168-175
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    • A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis
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    • Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • This is the first study to show that the TatBC complex binds substrate proteins
    • Cline, K. & Mori, H. Thylakoid ΔpH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J. Cell Biol. 154, 719-729 (2001). This is the first study to show that the TatBC complex binds substrate proteins.
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    • Cline, K.1    Mori, H.2
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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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    • Gerard, F.1    Cline, K.2
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    • Shanmugham, A.1    Wong Fong Sang, H.W.2    Bollen, Y.J.3    Lill, H.4
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    • Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI
    • Bageshwar, U. K., Whitaker, N., Liang, F. C. & Musser, S. M. Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI. Mol. Microbiol. 74, 209-226 (2009).
    • (2009) Mol. Microbiol. , vol.74 , pp. 209-226
    • Bageshwar, U.K.1    Whitaker, N.2    Liang, F.C.3    Musser, S.M.4
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    • The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits of the Escherichia coli twin-arginine translocase
    • Papish, A. L., Ladner, C. L. & Turner, R. J. The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits of the Escherichia coli twin-arginine translocase. J. Biol. Chem. 278, 32501-32506 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 32501-32506
    • Papish, A.L.1    Ladner, C.L.2    Turner, R.J.3
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    • Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation
    • Kostecki, J. S., Li, H., Turner, R. J. & DeLisa, M. P. Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation. PLoS ONE 5, e9225 (2010).
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    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • This work uses site-specific crosslinking to show that TatC interacts with the signal peptide twin-arginine motif, whereas TatB contacts the entire signal sequence
    • Alami, M. et al. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 12, 937-946 (2003). This work uses site-specific crosslinking to show that TatC interacts with the signal peptide twin-arginine motif, whereas TatB contacts the entire signal sequence.
    • (2003) Mol. Cell , vol.12 , pp. 937-946
    • Alami, M.1
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    • Efficient twin arginine translocation (Tat) pathway transport of a precursor protein covalently anchored to its initial cpTatC binding site
    • Gerard, F. & Cline, K. Efficient twin arginine translocation (Tat) pathway transport of a precursor protein covalently anchored to its initial cpTatC binding site. J. Biol. Chem. 281, 6130-6135 (2006).
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    • Gerard, F.1    Cline, K.2
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    • TatB functions as an oligomeric binding site for folded Tat precursor proteins
    • Maurer, C., Panahandeh, S., Jungkamp, A. C., Moser, M. & Muller, M. TatB functions as an oligomeric binding site for folded Tat precursor proteins. Mol. Biol. Cell 21, 4151-4161 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4151-4161
    • Maurer, C.1    Panahandeh, S.2    Jungkamp, A.C.3    Moser, M.4    Muller, M.5
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    • Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides
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    • Mapping the precursor-binding site on the TatC subunit of the twin-arginine-specific protein translocase by site-specific photo cross-linking
    • Zoufaly, S. et al. Mapping the precursor-binding site on the TatC subunit of the twin-arginine-specific protein translocase by site-specific photo cross-linking. J. Biol. Chem. 287, 13430-13441 (2012).
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    • Kinetics of precursor interactions with the bacterial Tat translocase detected by real-time FRET
    • Whitaker, N., Bageshwar, U. K. & Musser, S. M. Kinetics of precursor interactions with the bacterial Tat translocase detected by real-time FRET. J. Biol. Chem. 287, 11252-11260 (2012).
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    • A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
    • This article demonstrates that thylakoid TatA interacts with the thylakoid TatBC complex only during substrate transport
    • Mori, H. & Cline, K. A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase. J. Cell Biol. 157, 205-210 (2002). This article demonstrates that thylakoid TatA interacts with the thylakoid TatBC complex only during substrate transport.
    • (2002) J. Cell Biol. , vol.157 , pp. 205-210
    • Mori, H.1    Cline, K.2
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    • Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coli
    • Panahandeh, S., Maurer, C., Moser, M., DeLisa, M. P. & Muller, M. Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coli. J. Biol. Chem. 283, 33267-33275 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 33267-33275
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  • 91
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    • Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
    • Dabney-Smith, C., Mori, H. & Cline, K. Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J. Biol. Chem. 281, 5476-5483 (2006).
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    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
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    • Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system
    • References 91 and 92 use chemical crosslinking to show that TatA polymerization is induced in thylakoids by the substrate-bound TatBC complex and by the PMF
    • Dabney-Smith, C. & Cline, K. Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system. Mol. Biol. Cell 20, 2060-2069 (2009). References 91 and 92 use chemical crosslinking to show that TatA polymerization is induced in thylakoids by the substrate-bound TatBC complex and by the PMF.
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    • Dabney-Smith, C.1    Cline, K.2
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    • Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging
    • This study uses in vivo imaging of fluorophore-tagged TatA to show that it forms large assemblies of variable stoichiometry in a TatBC-dependent manner
    • Leake, M. C. et al. Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging. Proc. Natl Acad. Sci. USA 105, 15376-15381 (2008). This study uses in vivo imaging of fluorophore-tagged TatA to show that it forms large assemblies of variable stoichiometry in a TatBC-dependent manner.
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    • Leake, M.C.1
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    • Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation
    • Frobel, J., Rose, P. & Muller, M. Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation. J. Biol. Chem. 286, 43679-43689 (2011).
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    • Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes
    • de Leeuw, E. et al. Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes. J. Mol. Biol. 322, 1135-1146 (2002).
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    • De Leeuw, E.1
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    • Two electrical potential-dependent steps are required for transport by the Escherichia coli Tat machinery
    • This article demonstrates that the electrical potential component of the PMF is required for two distinct steps in Tat-mediated transport
    • Bageshwar, U. K. & Musser, S. M. Two electrical potential-dependent steps are required for transport by the Escherichia coli Tat machinery. J. Cell Biol. 179, 87-99 (2007). This article demonstrates that the electrical potential component of the PMF is required for two distinct steps in Tat-mediated transport.
    • (2007) J. Cell Biol. , vol.179 , pp. 87-99
    • Bageshwar, U.K.1    Musser, S.M.2
  • 97
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    • Solution NMR structure of the TatA component of the twin-arginine protein transport system from Gram-positive bacterium Bacillus subtilis
    • This paper reports the solution NMR structure of the TMH and APH domains of a TatA protein
    • Hu, Y., Zhao, E., Li, H., Xia, B. & Jin, C. Solution NMR structure of the TatA component of the twin-arginine protein transport system from Gram-positive bacterium Bacillus subtilis. J. Am. Chem. Soc. 132, 15942-15944 (2010). This paper reports the solution NMR structure of the TMH and APH domains of a TatA protein.
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    • Sec-independent protein translocation by the maize Hcf106 protein
    • This article describes the identification of a protein component that is essential for protein transport by the plant Tat pathway, and the recognition that similar components are encoded in the genomes of bacteria
    • Settles, A. M. et al. Sec-independent protein translocation by the maize Hcf106 protein. Science 278, 1467-1470 (1997). This article describes the identification of a protein component that is essential for protein transport by the plant Tat pathway, and the recognition that similar components are encoded in the genomes of bacteria.
    • (1997) Science , vol.278 , pp. 1467-1470
    • Settles, A.M.1
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    • Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system
    • Porcelli, I. et al. Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system. Biochemistry 41, 13690-13697 (2002).
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    • Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation
    • Lee, P. A., Buchanan, G., Stanley, N. R., Berks, B. C. & Palmer, T. Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation. J. Bacteriol. 184, 5871-5879 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 5871-5879
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