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Volumn 60, Issue , 2006, Pages 373-395

The bacterial twin-arginine translocation pathway

Author keywords

Biotechnology; Pathogenesis; Protein transport; Tat; Translocase

Indexed keywords

AMINO ACID; CELL PROTEIN; PROTEIN SEC; PROTEIN TATA; PROTEIN TATB; PROTEIN TATC; SIGNAL PEPTIDASE I; SIGNAL PEPTIDE; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 33750381048     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.60.080805.142212     Document Type: Review
Times cited : (266)

References (137)
  • 1
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alami M, Luke I, Deitermann S, Eisner G, Koch HG, et al. 2003. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 12:937-46
    • (2003) Mol. Cell , vol.12 , pp. 937-946
    • Alami, M.1    Luke, I.2    Deitermann, S.3    Eisner, G.4    Koch, H.G.5
  • 2
    • 0037036383 scopus 로고    scopus 로고
    • Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli
    • Alami M, Trescher D, Wu LF, Muller M. 2002. Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli. J. Biol. Chem. 277:20499-503
    • (2002) J. Biol. Chem. , vol.277 , pp. 20499-20503
    • Alami, M.1    Trescher, D.2    Wu, L.F.3    Muller, M.4
  • 3
    • 0037462475 scopus 로고    scopus 로고
    • Energetics of protein transport across biological membranes. A study of the thylakoid DeltapH-dependent/cpTat pathway
    • Alder NN, Theg SM. 2003. Energetics of protein transport across biological membranes. A study of the thylakoid DeltapH-dependent/cpTat pathway. Cell 112:231-42
    • (2003) Cell , vol.112 , pp. 231-242
    • Alder, N.N.1    Theg, S.M.2
  • 4
    • 0041656271 scopus 로고    scopus 로고
    • Energy use by biological protein transport pathways
    • Alder NN, Theg SM. 2003. Energy use by biological protein transport pathways. Trends Biochem. Sci. 28:442-51
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 442-451
    • Alder, N.N.1    Theg, S.M.2
  • 5
    • 0037155803 scopus 로고    scopus 로고
    • Essential cytoplasmic domains in the Escherichia coli TatC protein
    • Allen SC, Barrett CM, Ray N, Robinson C. 2002. Essential cytoplasmic domains in the Escherichia coli TatC protein. J. Biol. Chem. 277:10362-66
    • (2002) J. Biol. Chem. , vol.277 , pp. 10362-10366
    • Allen, S.C.1    Barrett, C.M.2    Ray, N.3    Robinson, C.4
  • 6
    • 0037468404 scopus 로고    scopus 로고
    • Identification of key regions within the Escherichia coli TatAB subunits
    • Barrett CM, Mathers JE, Robinson C. 2003. Identification of key regions within the Escherichia coli TatAB subunits. FEBS Lett. 537:42-46
    • (2003) FEBS Lett. , vol.537 , pp. 42-46
    • Barrett, C.M.1    Mathers, J.E.2    Robinson, C.3
  • 7
    • 0037414423 scopus 로고    scopus 로고
    • Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli
    • Barrett CM, Ray N, Thomas JD, Robinson C, Bolhuis A. 2003. Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli. Biochem. Biophys. Res. Commun. 304:279-84
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 279-284
    • Barrett, C.M.1    Ray, N.2    Thomas, J.D.3    Robinson, C.4    Bolhuis, A.5
  • 8
    • 18444411638 scopus 로고    scopus 로고
    • Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin-arginine translocase
    • Barrett CM, Robinson C. 2005. Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin-arginine translocase. FEBS J. 272:2261-75
    • (2005) FEBS J. , vol.272 , pp. 2261-2275
    • Barrett, C.M.1    Robinson, C.2
  • 11
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks BC. 1996. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:393-404
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 12
    • 0141672034 scopus 로고    scopus 로고
    • The Tat protein translocation pathway and its role in microbial physiology
    • Berks BC, Palmer T, Sargent F. 2003. The Tat protein translocation pathway and its role in microbial physiology. Adv. Microb. Physiol. 47:187-254
    • (2003) Adv. Microb. Physiol. , vol.47 , pp. 187-254
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 13
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt TG, de Boer PA. 2003. The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol. Microbiol. 48:1171-82
    • (2003) Mol. Microbiol. , vol.48 , pp. 1171-1182
    • Bernhardt, T.G.1    De Boer, P.A.2
  • 14
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette PH, Aslund F, Beckwith J, Georgiou G. 1999. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. USA 96:13703-8
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 15
    • 0037407866 scopus 로고    scopus 로고
    • Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane
    • Blaudeck N, Kreutzenbeck P, Freudl R, Sprenger GA. 2003. Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane. J. Bacteriol. 185:2811-19
    • (2003) J. Bacteriol. , vol.185 , pp. 2811-2819
    • Blaudeck, N.1    Kreutzenbeck, P.2    Freudl, R.3    Sprenger, G.A.4
  • 16
    • 13544249592 scopus 로고    scopus 로고
    • Isolation and characterization of bifunctional Escherichia coli TatA mutant proteins that allow efficient Tat-dependent protein translocation in the absence of TatB
    • Blaudeck N, Kreutzenbeck P, Muller M, Sprenger GA, Freudl R. 2005. Isolation and characterization of bifunctional Escherichia coli TatA mutant proteins that allow efficient Tat-dependent protein translocation in the absence of TatB. J. Biol. Chem. 280:3426-32
    • (2005) J. Biol. Chem. , vol.280 , pp. 3426-3432
    • Blaudeck, N.1    Kreutzenbeck, P.2    Muller, M.3    Sprenger, G.A.4    Freudl, R.5
  • 17
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • Bogsch EG, Sargent F, Stanley NR, Berks BC, Robinson C, Palmer T. 1998. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J. Biol. Chem. 273:18003-6
    • (1998) J. Biol. Chem. , vol.273 , pp. 18003-18006
    • Bogsch, E.G.1    Sargent, F.2    Stanley, N.R.3    Berks, B.C.4    Robinson, C.5    Palmer, T.6
  • 18
    • 0034697250 scopus 로고    scopus 로고
    • Subunit interactions in the twin-arginine translocase complex of Escherichia coli
    • Bolhuis A, Bogsch EG, Robinson C. 2000. Subunit interactions in the twin-arginine translocase complex of Escherichia coli. FEBS Lett. 472:88-92
    • (2000) FEBS Lett. , vol.472 , pp. 88-92
    • Bolhuis, A.1    Bogsch, E.G.2    Robinson, C.3
  • 19
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • Bolhuis A, Mathers JE, Thomas JD, Barrett CM, Robinson C. 2001. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 276:20213-19
    • (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
  • 20
    • 9644266608 scopus 로고    scopus 로고
    • Dissecting the twin-arginine translocation pathway using genome-wide analysis
    • Bronstein P, Marrichi M, DeLisa MP. 2004. Dissecting the twin-arginine translocation pathway using genome-wide analysis. Res. Microbiol. 155:803-10
    • (2004) Res. Microbiol. , vol.155 , pp. 803-810
    • Bronstein, P.1    Marrichi, M.2    DeLisa, M.P.3
  • 21
    • 28844461575 scopus 로고    scopus 로고
    • Identification of a twin-arginine translocation system in Pseudomonas syringae pv. tomato DC3000 and its contribution to pathogenicity and fitness
    • Bronstein PA, Marrichi M, Cartinhour S, Schneider DJ, Delisa MP. 2005. Identification of a twin-arginine translocation system in Pseudomonas syringae pv. tomato DC3000 and its contribution to pathogenicity and fitness. J. Bacteriol. 187:8450-61
    • (2005) J. Bacteriol. , vol.187 , pp. 8450-8461
    • Bronstein, P.A.1    Marrichi, M.2    Cartinhour, S.3    Schneider, D.J.4    Delisa, M.P.5
  • 22
    • 0036274596 scopus 로고    scopus 로고
    • Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
    • Buchanan G, Leeuw E, Stanley NR, Wexler M, Berks BC, et al. 2002. Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis. Mol. Microbiol. 43:1457-70
    • (2002) Mol. Microbiol. , vol.43 , pp. 1457-1470
    • Buchanan, G.1    Leeuw, E.2    Stanley, N.R.3    Wexler, M.4    Berks, B.C.5
  • 23
    • 0036136514 scopus 로고    scopus 로고
    • A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif
    • Buchanan G, Sargent F, Berks BC, Palmer T. 2001. A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif. Arch. Microbiol. 177:107-12
    • (2001) Arch. Microbiol. , vol.177 , pp. 107-112
    • Buchanan, G.1    Sargent, F.2    Berks, B.C.3    Palmer, T.4
  • 24
    • 31644447233 scopus 로고    scopus 로고
    • The Tat pathway of the plant pathogen Pseudomonas syringae is required for optimal virulence
    • Caldelari I, Mann S, Crooks C, Palmer T. 2006. The Tat pathway of the plant pathogen Pseudomonas syringae is required for optimal virulence. Mol. Plant. Microbe Interact. 19:200-12
    • (2006) Mol. Plant. Microbe Interact. , vol.19 , pp. 200-212
    • Caldelari, I.1    Mann, S.2    Crooks, C.3    Palmer, T.4
  • 25
    • 27844506497 scopus 로고    scopus 로고
    • Type II secretion: A protein secretion system for all seasons
    • Cianciotto NP. 2005. Type II secretion: a protein secretion system for all seasons. Trends Microbiol. 13:581-88
    • (2005) Trends Microbiol. , vol.13 , pp. 581-588
    • Cianciotto, N.P.1
  • 26
    • 0026787702 scopus 로고
    • Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP
    • Cline K, Ettinger WF, Theg SM. 1992. 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. 267:2688-96
    • (1992) J. Biol. Chem. , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.F.2    Theg, S.M.3
  • 27
    • 0035920363 scopus 로고    scopus 로고
    • Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • Cline K, Mori H. 2001. Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J. Cell Biol. 154:719-29
    • (2001) J. Cell Biol. , vol.154 , pp. 719-729
    • Cline, K.1    Mori, H.2
  • 28
    • 0028945041 scopus 로고
    • A monomeric, tightly folded stromal intermediate on the delta pH-dependent thylakoidal protein transport pathway
    • Creighton AM, Hulford A, Mant A, Robinson D, Robinson C. 1995. A monomeric, tightly folded stromal intermediate on the delta pH-dependent thylakoidal protein transport pathway. J. Biol. Chem. 270:1663-69
    • (1995) J. Biol. Chem. , vol.270 , pp. 1663-1669
    • Creighton, A.M.1    Hulford, A.2    Mant, A.3    Robinson, D.4    Robinson, C.5
  • 29
    • 0040537042 scopus 로고    scopus 로고
    • Competition between Sec- and TAT-dependent protein translocation in Escherichia coli
    • Cristobal S, de Gier JW, Nielsen H, von Heijne G. 1999. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 18:2982-90
    • (1999) EMBO J. , vol.18 , pp. 2982-2990
    • Cristobal, S.1    De Gier, J.W.2    Nielsen, H.3    Von Heijne, G.4
  • 30
    • 0242290351 scopus 로고    scopus 로고
    • Requirement of a Tha4-conserved transmembrane glutamate in thylakoid Tat translocase assembly revealed by biochemical complementation
    • Dabney-Smith C, Mori H, Cline K. 2003. Requirement of a Tha4-conserved transmembrane glutamate in thylakoid Tat translocase assembly revealed by biochemical complementation. J. Biol. Chem. 278:43027-33
    • (2003) J. Biol. Chem. , vol.278 , pp. 43027-43033
    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
  • 31
    • 22644441730 scopus 로고    scopus 로고
    • The phage-shock-protein response
    • Darwin AJ. 2005. The phage-shock-protein response. Mol. Microbiol. 57:621-28
    • (2005) Mol. Microbiol. , vol.57 , pp. 621-628
    • Darwin, A.J.1
  • 33
    • 18844365360 scopus 로고    scopus 로고
    • Legionella pneumophila Philadelphia-1 tatB and tatC affect intracellular replication and biofilm formation
    • De Buck E, Maes L, Meyen E, Van Mellaert L, Geukens N, et al. 2005. Legionella pneumophila Philadelphia-1 tatB and tatC affect intracellular replication and biofilm formation. Biochem. Biophys. Res. Commun. 331:1413-20
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1413-1420
    • De Buck, E.1    Maes, L.2    Meyen, E.3    Van Mellaert, L.4    Geukens, N.5
  • 34
    • 0036412417 scopus 로고    scopus 로고
    • Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes
    • De Leeuw E, Granjon T, Porcelli I, Alami M, Carr SB, et al. 2002. Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes. J. Mol. Biol. 322:1135-46
    • (2002) J. Mol. Biol. , vol.322 , pp. 1135-1146
    • De Leeuw, E.1    Granjon, T.2    Porcelli, I.3    Alami, M.4    Carr, S.B.5
  • 35
    • 0035812905 scopus 로고    scopus 로고
    • Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway
    • De Leeuw E, Porcelli I, Sargent F, Palmer T, Berks BC. 2001. Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. FEBS Lett. 506:143-48
    • (2001) FEBS Lett. , vol.506 , pp. 143-148
    • De Leeuw, E.1    Porcelli, I.2    Sargent, F.3    Palmer, T.4    Berks, B.C.5
  • 36
    • 0346655242 scopus 로고    scopus 로고
    • Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway
    • DeLisa MP, Lee P, Palmer T, Georgiou G. 2004. Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway. J. Bacteriol. 186:366-73
    • (2004) J. Bacteriol. , vol.186 , pp. 366-373
    • DeLisa, M.P.1    Lee, P.2    Palmer, T.3    Georgiou, G.4
  • 37
    • 0037119435 scopus 로고    scopus 로고
    • Genetic analysis of the twin arginine translocator secretion pathway in bacteria
    • DeLisa MP, Samuelson P, Palmer T, Georgiou G. 2002. Genetic analysis of the twin arginine translocator secretion pathway in bacteria. J. Biol. Chem. 277:29825-31
    • (2002) J. Biol. Chem. , vol.277 , pp. 29825-29831
    • Delisa, M.P.1    Samuelson, P.2    Palmer, T.3    Georgiou, G.4
  • 38
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa MP, Tullman D, Georgiou G. 2003. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci. USA 100:6115-20
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 39
    • 29244476252 scopus 로고    scopus 로고
    • The thylakoid ΔpH/Δpsi are not required for the initial stages of Tat-dependent protein transport in tobacco protoplasts
    • Di Cola A, Bailey S, Robinson C. 2005. The thylakoid ΔpH/Δpsi are not required for the initial stages of Tat-dependent protein transport in tobacco protoplasts. J. Biol. Chem. 280:41165-70
    • (2005) J. Biol. Chem. , vol.280 , pp. 41165-41170
    • Di Cola, A.1    Bailey, S.2    Robinson, C.3
  • 40
    • 27544470676 scopus 로고    scopus 로고
    • Large-scale translocation reversal within the thylakoid Tat system in vivo
    • Di Cola A, Robinson C. 2005. Large-scale translocation reversal within the thylakoid Tat system in vivo. J. Cell Biol. 171:281-89
    • (2005) J. Cell Biol. , vol.171 , pp. 281-289
    • Di Cola, A.1    Robinson, C.2
  • 41
    • 27844443566 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea
    • Dilks K, Gimenez MI, Pohlschroder M. 2005. Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea. J. Bacteriol. 187:8104-13
    • (2005) J. Bacteriol. , vol.187 , pp. 8104-8113
    • Dilks, K.1    Gimenez, M.I.2    Pohlschroder, M.3
  • 42
    • 0037317124 scopus 로고    scopus 로고
    • Prokaryotic utilization of the twin-arginine translocation pathway: A genomic survey
    • Dilks K, Rose RW, Hartmann E, Pohlschroder M. 2003. Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey. J. Bacteriol. 185:1478-83
    • (2003) J. Bacteriol. , vol.185 , pp. 1478-1483
    • Dilks, K.1    Rose, R.W.2    Hartmann, E.3    Pohlschroder, M.4
  • 43
    • 0037307748 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens twin-arginine-dependent translocation is important for virulence, flagellation, and chemotaxis but not type IV secretion
    • Ding Z, Christie PJ. 2003. Agrobacterium tumefaciens twin-arginine- dependent translocation is important for virulence, flagellation, and chemotaxis but not type IV secretion. J. Bacteriol. 185:760-71
    • (2003) J. Bacteriol. , vol.185 , pp. 760-771
    • Ding, Z.1    Christie, P.J.2
  • 44
    • 0042564757 scopus 로고    scopus 로고
    • Assembly of Tat-dependent [NiFe] hydrogenases: Identification of precursor-binding accessory proteins
    • Dubini A, Sargent F. 2003. Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins. FEBS Lett. 549:141-46
    • (2003) FEBS Lett. , vol.549 , pp. 141-146
    • Dubini, A.1    Sargent, F.2
  • 45
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in Escherichia coli
    • Feilmeier BJ, Iseminger G, Schroeder D, Webber H, Phillips GJ. 2000. Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J. Bacteriol. 182:4068-76
    • (2000) J. Bacteriol. , vol.182 , pp. 4068-4076
    • Feilmeier, B.J.1    Iseminger, G.2    Schroeder, D.3    Webber, H.4    Phillips, G.J.5
  • 46
    • 0037450644 scopus 로고    scopus 로고
    • Thylakoid targeting of Tat passenger proteins shows no ΔpH dependence in vivo
    • Finazzi G, Chasen C, Wollman FA, de Vitry C. 2003. Thylakoid targeting of Tat passenger proteins shows no ΔpH dependence in vivo. EMBO J. 22:807-15
    • (2003) EMBO J. , vol.22 , pp. 807-815
    • Finazzi, G.1    Chasen, C.2    Wollman, F.A.3    De Vitry, C.4
  • 47
    • 33644536727 scopus 로고    scopus 로고
    • Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway
    • Fisher AC, Kim W, DeLisa MP. 2006. Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway. Protein Sci. 15:449-58
    • (2006) Protein Sci. , vol.15 , pp. 449-458
    • Fisher, A.C.1    Kim, W.2    Delisa, M.P.3
  • 48
    • 0027425230 scopus 로고
    • Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface
    • Francisco JA, Campbell R, Iverson BL, Georgiou G. 1993. Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface. Proc. Natl. Acad. Sci. USA 90:10444-48
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10444-10448
    • Francisco, J.A.1    Campbell, R.2    Iverson, B.L.3    Georgiou, G.4
  • 49
    • 20444408697 scopus 로고    scopus 로고
    • Increase in xylanase production by Streptomyces lividans through simultaneous use of the Sec- and Tat-dependent protein export systems
    • Gauthier C, Li H, Morosoli R. 2005. Increase in xylanase production by Streptomyces lividans through simultaneous use of the Sec- and Tat-dependent protein export systems. Appl. Environ. Microbiol. 71:3085-92
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 3085-3092
    • Gauthier, C.1    Li, H.2    Morosoli, R.3
  • 50
    • 0000598585 scopus 로고    scopus 로고
    • Respiration
    • ed. FC Neidhardt, R Curtiss III, JL Ingraham, ECC Lin, KB Low. Washington, DC: Am. Soc. Microbiol. 2nd ed.
    • Gennis RB, Stewart V. 1996. Respiration. In Escherichia coli and Salmonella: Cellular and Molecular Biology, ed. FC Neidhardt, R Curtiss III, JL Ingraham, ECC Lin, KB Low, pp. 217-61. Washington, DC: Am. Soc. Microbiol. 2nd ed.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 217-261
    • Gennis, R.B.1    Stewart, V.2
  • 51
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: Status report and future prospects
    • Georgiou G, Segatori L. 2005. Preparative expression of secreted proteins in bacteria: status report and future prospects. Curr. Opin. Biotechnol. 16:538-45
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 52
    • 23044487649 scopus 로고    scopus 로고
    • The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter
    • Gohlke U, Pullan L, McDevitt CA, Porcelli I, de Leeuw E, et al. 2005. The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter. Proc. Natl. Acad. Sci. USA 102:10482-86
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10482-10486
    • Gohlke, U.1    Pullan, L.2    McDevitt, C.A.3    Porcelli, I.4    De Leeuw, E.5
  • 53
    • 1642523788 scopus 로고    scopus 로고
    • Dual topology of the Escherichia coli TatA protein
    • Gouffi K, Gerard F, Santini CL, Wu LF. 2004. Dual topology of the Escherichia coli TatA protein. J. Biol. Chem. 279:11608-15
    • (2004) J. Biol. Chem. , vol.279 , pp. 11608-11615
    • Gouffi, K.1    Gerard, F.2    Santini, C.L.3    Wu, L.F.4
  • 54
    • 3042647616 scopus 로고    scopus 로고
    • Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries
    • Harvey BR, Georgiou G, Hayhurst A, Jeong KJ, Iverson BL, Rogers GK. 2004. Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries. Proc. Natl. Acad. Sci. USA 101:9193-98
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9193-9198
    • Harvey, B.R.1    Georgiou, G.2    Hayhurst, A.3    Jeong, K.J.4    Iverson, B.L.5    Rogers, G.K.6
  • 56
    • 0141789788 scopus 로고    scopus 로고
    • A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase
    • Hatzixanthis K, Palmer T, Sargent F. 2003. A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase. Mol. Microbiol. 49:1377-90
    • (2003) Mol. Microbiol. , vol.49 , pp. 1377-1390
    • Hatzixanthis, K.1    Palmer, T.2    Sargent, F.3
  • 57
    • 0037468635 scopus 로고    scopus 로고
    • The Escherichia coli twin-arginine translocase: Conserved residues of TatA and TatB family components involved in protein transport
    • Hicks MG, de Leeuw E, Porcelli I, Buchanan G, Berks BC, Palmer T. 2003. The Escherichia coli twin-arginine translocase: conserved residues of TatA and TatB family components involved in protein transport. FEBS Lett. 539:61-67
    • (2003) FEBS Lett. , vol.539 , pp. 61-67
    • Hicks, M.G.1    De Leeuw, E.2    Porcelli, I.3    Buchanan, G.4    Berks, B.C.5    Palmer, T.6
  • 58
    • 14644444922 scopus 로고    scopus 로고
    • Positive selection for loss-of-function tat mutations identifies critical residues required for TatA activity
    • Hicks MG, Lee PA, Georgiou G, Berks BC, Palmer T. 2005. Positive selection for loss-of-function tat mutations identifies critical residues required for TatA activity. J. Bacteriol. 187:2920-25
    • (2005) J. Bacteriol. , vol.187 , pp. 2920-2925
    • Hicks, M.G.1    Lee, P.A.2    Georgiou, G.3    Berks, B.C.4    Palmer, T.5
  • 59
    • 0036854448 scopus 로고    scopus 로고
    • Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica
    • Hinsley AP, Berks BC. 2002. Specificity of respiratory pathways involved in the reduction of sulfur compounds by Salmonella enterica. Microbiology 148:3631-38
    • (2002) Microbiology , vol.148 , pp. 3631-3638
    • Hinsley, A.P.1    Berks, B.C.2
  • 60
    • 0035907063 scopus 로고    scopus 로고
    • A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif
    • Hinsley AP, Stanley NR, Palmer T, Berks BC. 2001. A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif. FEBS Lett. 497:45-49
    • (2001) FEBS Lett. , vol.497 , pp. 45-49
    • Hinsley, A.P.1    Stanley, N.R.2    Palmer, T.3    Berks, B.C.4
  • 61
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom HR. 2005. Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 23:1105-16
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 62
    • 17644386832 scopus 로고    scopus 로고
    • Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation
    • Huber D, Boyd D, Xia Y, Olma MH, Gerstein M, Beckwith J. 2005. Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation. J. Bacteriol. 187:2983-91
    • (2005) J. Bacteriol. , vol.187 , pp. 2983-2991
    • Huber, D.1    Boyd, D.2    Xia, Y.3    Olma, M.H.4    Gerstein, M.5    Beckwith, J.6
  • 63
    • 0038202125 scopus 로고    scopus 로고
    • The archaeal twin-arginine translocation pathway
    • Hutcheon GW, Bolhuis A. 2003. The archaeal twin-arginine translocation pathway. Biochem. Soc. Trans. 31:686-89
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 686-689
    • Hutcheon, G.W.1    Bolhuis, A.2
  • 64
    • 0036088769 scopus 로고    scopus 로고
    • Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery
    • Ignatova Z, Hornle C, Nurk A, Kasche V. 2002. Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery. Biochem. Biophys. Res. Commun. 291:146-49
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 146-149
    • Ignatova, Z.1    Hornle, C.2    Nurk, A.3    Kasche, V.4
  • 65
    • 1942505361 scopus 로고    scopus 로고
    • Functional and structural analysis of members of the TorD family, a large chaperone family dedicated to molybdoproteins
    • Ilbert M, Mejean V, Iobbi-Nivol C. 2004. Functional and structural analysis of members of the TorD family, a large chaperone family dedicated to molybdoproteins. Microbiology 150:935-13
    • (2004) Microbiology , vol.150 , pp. 935-13
    • Ilbert, M.1    Mejean, V.2    Iobbi-Nivol, C.3
  • 66
    • 0036431451 scopus 로고    scopus 로고
    • In vivo assessment of the Tat signal peptide specificity in Escherichia coli
    • Ize B, Gerard F, Wu LF. 2002. In vivo assessment of the Tat signal peptide specificity in Escherichia coli. Arch. Microbiol. 178:548-53
    • (2002) Arch. Microbiol. , vol.178 , pp. 548-553
    • Ize, B.1    Gerard, F.2    Wu, L.F.3
  • 67
    • 0036296099 scopus 로고    scopus 로고
    • In vivo dissection of the Tat translocation pathway in Escherichia coli
    • Ize B, Gerard F, Zhang M, Chanal A, Voulhoux R, et al. 2002. In vivo dissection of the Tat translocation pathway in Escherichia coli. J. Mol. Biol. 317:327-35
    • (2002) J. Mol. Biol. , vol.317 , pp. 327-335
    • Ize, B.1    Gerard, F.2    Zhang, M.3    Chanal, A.4    Voulhoux, R.5
  • 68
    • 9144251714 scopus 로고    scopus 로고
    • Novel phenotypes of Escherichia coli tat mutants revealed by global gene expression and phenotypic analysis
    • Ize B, Porcelli I, Lucchini S, Hinton JC, Berks BC, Palmer T. 2004. Novel phenotypes of Escherichia coli tat mutants revealed by global gene expression and phenotypic analysis. J. Biol. Chem. 279:47543-54
    • (2004) J. Biol. Chem. , vol.279 , pp. 47543-47554
    • Ize, B.1    Porcelli, I.2    Lucchini, S.3    Hinton, J.C.4    Berks, B.C.5    Palmer, T.6
  • 69
    • 0038460119 scopus 로고    scopus 로고
    • Role of the Escherichia coli Tat pathway in outer membrane integrity
    • Ize B, Stanley NR, Buchanan G, Palmer T. 2003. Role of the Escherichia coli Tat pathway in outer membrane integrity. Mol. Microbiol. 48:1183-93
    • (2003) Mol. Microbiol. , vol.48 , pp. 1183-1193
    • Ize, B.1    Stanley, N.R.2    Buchanan, G.3    Palmer, T.4
  • 71
    • 0035118223 scopus 로고    scopus 로고
    • Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth
    • Jack RL, Sargent F, Berks BC, Sawers G, Palmer T. 2001. Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth. J. Bacteriol. 183:1801-4
    • (2001) J. Bacteriol. , vol.183 , pp. 1801-1804
    • Jack, R.L.1    Sargent, F.2    Berks, B.C.3    Sawers, G.4    Palmer, T.5
  • 72
    • 11244280828 scopus 로고    scopus 로고
    • Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in Tat-mediated export
    • Jong WS, ten Hagen-Jongman CM, Genevaux P, Brunner J, Oudega B, Luirink J. 2004. Trigger factor interacts with the signal peptide of nascent Tat substrates but does not play a critical role in Tat-mediated export. Eur. J. Biochem. 271:4779-87
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4779-4787
    • Jong, W.S.1    Ten Hagen-Jongman, C.M.2    Genevaux, P.3    Brunner, J.4    Oudega, B.5    Luirink, J.6
  • 73
    • 0348150717 scopus 로고    scopus 로고
    • Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis
    • Jongbloed JD, Antelmann H, Hecker M, Nijland R, Bron S, et al. 2002. Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis. J. Biol. Chem. 277:44068-78
    • (2002) J. Biol. Chem. , vol.277 , pp. 44068-44078
    • Jongbloed, J.D.1    Antelmann, H.2    Hecker, M.3    Nijland, R.4    Bron, S.5
  • 75
    • 0034731394 scopus 로고    scopus 로고
    • TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway
    • Jongbloed JD, Martin U, Antelmann H, Hecker M, Tjalsma H, et al. 2000. TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway. J. Biol. Chem. 275:41350-57
    • (2000) J. Biol. Chem. , vol.275 , pp. 41350-41357
    • Jongbloed, J.D.1    Martin, U.2    Antelmann, H.3    Hecker, M.4    Tjalsma, H.5
  • 76
    • 23044481815 scopus 로고    scopus 로고
    • Functional periplasmic secretion of organophosphorous hydrolase using the twin-arginine translocation pathway in Escherichia coli
    • Kang DG, Lim GB, Cha HJ. 2005. Functional periplasmic secretion of organophosphorous hydrolase using the twin-arginine translocation pathway in Escherichia coli. J. Biotechnol. 118:379-85
    • (2005) J. Biotechnol. , vol.118 , pp. 379-385
    • Kang, D.G.1    Lim, G.B.2    Cha, H.J.3
  • 77
    • 3843140548 scopus 로고    scopus 로고
    • A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis
    • Ki JJ, Kawarasaki Y, Gam J, Harvey BR, Iverson BL, Georgiou G. 2004. A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis. J. Mol. Biol. 341:901-9
    • (2004) J. Mol. Biol. , vol.341 , pp. 901-909
    • Ki, J.J.1    Kawarasaki, Y.2    Gam, J.3    Harvey, B.R.4    Iverson, B.L.5    Georgiou, G.6
  • 78
    • 29144447051 scopus 로고    scopus 로고
    • Twin-arginine translocation of active human tissue plasminogen activator in Escherichia coli
    • Kim JY, Fogarty EA, Lu FJ, Zhu H, Wheelock GD, et al. 2005. Twin-arginine translocation of active human tissue plasminogen activator in Escherichia coli. Appl. Environ. Microbiol. 71:8451-59
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 8451-8459
    • Kim, J.Y.1    Fogarty, E.A.2    Lu, F.J.3    Zhu, H.4    Wheelock, G.D.5
  • 79
    • 0036837744 scopus 로고    scopus 로고
    • Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation
    • Lee PA, Buchanan G, Stanley NR, Berks BC, Palmer T. 2002. Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation. J. Bacteriol. 184:5871-79
    • (2002) J. Bacteriol. , vol.184 , pp. 5871-5879
    • Lee, P.A.1    Buchanan, G.2    Stanley, N.R.3    Berks, B.C.4    Palmer, T.5
  • 80
    • 22144492215 scopus 로고    scopus 로고
    • Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins
    • Li H, Jacques PE, Ghinet MG, Brzezinski R, Morosoli R. 2005. Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins. Microbiology 151:2189-98
    • (2005) Microbiology , vol.151 , pp. 2189-2198
    • Li, H.1    Jacques, P.E.2    Ghinet, M.G.3    Brzezinski, R.4    Morosoli, R.5
  • 81
    • 33645365498 scopus 로고    scopus 로고
    • Coexpression of TorD enhances the transport of GFP via the TAT pathway
    • Li SY, Chang BY, Lin SC. 2005. Coexpression of TorD enhances the transport of GFP via the TAT pathway. J. Biotechnol. 1224:412-21
    • (2005) J. Biotechnol. , vol.1224 , pp. 412-421
    • Li, S.Y.1    Chang, B.Y.2    Lin, S.C.3
  • 82
    • 9644273939 scopus 로고    scopus 로고
    • The core TatABC complex of the twin-arginine translocase in Escherichia coli: TatC drives assembly whereas TatA is essential for stability
    • Mangels D, Mathers J, Bolhuis A, Robinson C. 2005. The core TatABC complex of the twin-arginine translocase in Escherichia coli: TatC drives assembly whereas TatA is essential for stability. J. Mol. Biol. 345:415-23
    • (2005) J. Mol. Biol. , vol.345 , pp. 415-423
    • Mangels, D.1    Mathers, J.2    Bolhuis, A.3    Robinson, C.4
  • 83
    • 27744493918 scopus 로고    scopus 로고
    • The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases
    • McDonough JA, Hacker KE, Flores AR, Pavelka MSJ, Braunstein M. 2005. The twin-arginine translocation pathway of Mycobacterium smegmatis is functional and required for the export of mycobacterial beta-lactamases. J. Bacteriol. 187:7667-79
    • (2005) J. Bacteriol. , vol.187 , pp. 7667-7679
    • McDonough, J.A.1    Hacker, K.E.2    Flores, A.R.3    Pavelka, M.S.J.4    Braunstein, M.5
  • 84
    • 0035900736 scopus 로고    scopus 로고
    • The Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts: Missing link in the evolution of protein transport pathways in chloroplasts?
    • Molik S, Karnauchov I, Weidlich C, Herrmann RG, Klosgen RB. 2001. The Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts: missing link in the evolution of protein transport pathways in chloroplasts? J. Biol. Chem. 276:42761-66
    • (2001) J. Biol. Chem. , vol.276 , pp. 42761-42766
    • Molik, S.1    Karnauchov, I.2    Weidlich, C.3    Herrmann, R.G.4    Klosgen, R.B.5
  • 85
    • 0037092039 scopus 로고    scopus 로고
    • A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
    • Mori H, Cline K. 2002. A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase. J. Cell Biol. 157:205-10
    • (2002) J. Cell Biol. , vol.157 , pp. 205-210
    • Mori, H.1    Cline, K.2
  • 86
    • 0025781325 scopus 로고
    • A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane
    • Mould RM, Robinson C. 1991. A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J. Biol. Chem. 266:12189-93
    • (1991) J. Biol. Chem. , vol.266 , pp. 12189-12193
    • Mould, R.M.1    Robinson, C.2
  • 87
    • 0034682620 scopus 로고    scopus 로고
    • Proton transfer limits protein translocation rate by the thylakoid DeltapH/Tat machinery
    • Musser SM, Theg SM. 2000. Proton transfer limits protein translocation rate by the thylakoid DeltapH/Tat machinery. Biochemistry 39:8228-33
    • (2000) Biochemistry , vol.39 , pp. 8228-8233
    • Musser, S.M.1    Theg, S.M.2
  • 88
    • 0030013237 scopus 로고    scopus 로고
    • prlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors
    • Nouwen N, de Kruijff B, Tommassen J. 1996. prlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors. Proc. Natl. Acad. Sci. USA 93:5953-57
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5953-5957
    • Nouwen, N.1    De Kruijff, B.2    Tommassen, J.3
  • 89
    • 12344296658 scopus 로고    scopus 로고
    • The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex
    • Oates J, Barrett CM, Barnett JP, Byrne KG, Bolhuis A, Robinson C. 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. Mol. Biol. 346:295-305
    • (2005) J. Mol. Biol. , vol.346 , pp. 295-305
    • Oates, J.1    Barrett, C.M.2    Barnett, J.P.3    Byrne, K.G.4    Bolhuis, A.5    Robinson, C.6
  • 91
    • 0037062507 scopus 로고    scopus 로고
    • Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis
    • Ochsner UA, Snyder A, Vasil AI, Vasil ML. 2002. Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis. Proc. Natl. Acad. Sci. USA 99:8312-17
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8312-8317
    • Ochsner, U.A.1    Snyder, A.2    Vasil, A.I.3    Vasil, M.L.4
  • 92
    • 0037195612 scopus 로고    scopus 로고
    • Molecular hydrogen as an energy source for Helicobacter pylori
    • Olson JW, Maier RJ. 2002. Molecular hydrogen as an energy source for Helicobacter pylori. Science 298:1788-90
    • (2002) Science , vol.298 , pp. 1788-1790
    • Olson, J.W.1    Maier, R.J.2
  • 93
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik IJ, Ladner CL, Turner RJ. 2001. Identification of a twin-arginine leader-binding protein. Mol. Microbiol. 40:323-31
    • (2001) Mol. Microbiol. , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 94
    • 0024987613 scopus 로고
    • Molecular comparison of a nonhemolytic and a hemolytic phospholipase C from Pseudomonas aeruginosa
    • Ostroff RM, Vasil AI, Vasil ML. 1990. Molecular comparison of a nonhemolytic and a hemolytic phospholipase C from Pseudomonas aeruginosa. J. Bacteriol. 172:5915-23
    • (1990) J. Bacteriol. , vol.172 , pp. 5915-5923
    • Ostroff, R.M.1    Vasil, A.I.2    Vasil, M.L.3
  • 95
    • 16244380460 scopus 로고    scopus 로고
    • Export of complex cofactor-containing proteins by the bacterial Tat pathway
    • Palmer T, Sargent F, Berks BC. 2005. Export of complex cofactor-containing proteins by the bacterial Tat pathway. Trends Microbiol. 13:175-80
    • (2005) Trends Microbiol. , vol.13 , pp. 175-180
    • Palmer, T.1    Sargent, F.2    Berks, B.C.3
  • 96
    • 0042859766 scopus 로고    scopus 로고
    • The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits of the Escherichia coli twin-arginine translocase
    • Papish AL, Ladner CL, Turner RJ. 2003. The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits of the Escherichia coli twin-arginine translocase. J. Biol. Chem. 278:32501-6
    • (2003) J. Biol. Chem. , vol.278 , pp. 32501-32506
    • Papish, A.L.1    Ladner, C.L.2    Turner, R.J.3
  • 97
    • 17044426359 scopus 로고    scopus 로고
    • A twin-arginine translocation (Tat)-mediated phage display system
    • Paschke M, Hohne W. 2005. A twin-arginine translocation (Tat)-mediated phage display system. Gene 350:79-88
    • (2005) Gene , vol.350 , pp. 79-88
    • Paschke, M.1    Hohne, W.2
  • 98
    • 0032568823 scopus 로고    scopus 로고
    • TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli
    • Pommier J, Mejean V, Giordano G, Iobbi-Nivol C. 1998. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli. J. Biol. Chem. 273:16615-20
    • (1998) J. Biol. Chem. , vol.273 , pp. 16615-16620
    • Pommier, J.1    Mejean, V.2    Giordano, G.3    Iobbi-Nivol, C.4
  • 99
    • 0036479116 scopus 로고    scopus 로고
    • The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system
    • Pop O, Martin U, Abel C, Muller JP. 2002. The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system. J. Biol. Chem. 277:3268-73
    • (2002) J. Biol. Chem. , vol.277 , pp. 3268-3273
    • Pop, O.1    Martin, U.2    Abel, C.3    Muller, J.P.4
  • 100
    • 0141866853 scopus 로고    scopus 로고
    • Sequencespecific binding of prePhoD to soluble TatAd indicates protein-mediated targeting of the Tat export in Bacillus subtilis
    • Pop OI, Westermann M, Volkmer-Engert R, Schulz D, Lemke C, et al. 2003. Sequencespecific binding of prePhoD to soluble TatAd indicates protein-mediated targeting of the Tat export in Bacillus subtilis. J. Biol. Chem. 278:38428-36
    • (2003) J. Biol. Chem. , vol.278 , pp. 38428-38436
    • Pop, O.I.1    Westermann, M.2    Volkmer-Engert, R.3    Schulz, D.4    Lemke, C.5
  • 101
    • 0037137255 scopus 로고    scopus 로고
    • Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system
    • Porcelli I, de Leeuw E, Wallis R, van den Brink-van der Laan E, de Kruijff B, et al. 2002. Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system. Biochemistry 41:13690-97
    • (2002) Biochemistry , vol.41 , pp. 13690-13697
    • Porcelli, I.1    De Leeuw, E.2    Wallis, R.3    Van Den Brink-van Der Laan, E.4    De Kruijff, B.5
  • 102
    • 0042825530 scopus 로고    scopus 로고
    • Contribution of the twin arginine translocation system to the virulence of enterohemorrhagic Escherichia coli O157:H7
    • Pradel N, Ye C, Livrelli V, Xu J, Joly B, Wu LF. 2003. Contribution of the twin arginine translocation system to the virulence of enterohemorrhagic Escherichia coli O157:H7. Infect. Immun. 71:4908-16
    • (2003) Infect. Immun. , vol.71 , pp. 4908-4916
    • Pradel, N.1    Ye, C.2    Livrelli, V.3    Xu, J.4    Joly, B.5    Wu, L.F.6
  • 103
    • 0037448423 scopus 로고    scopus 로고
    • DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus
    • Ray N, Oates J, Turner RJ, Robinson C. 2003. DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus. FEBS Lett. 534:156-60
    • (2003) FEBS Lett. , vol.534 , pp. 156-160
    • Ray, N.1    Oates, J.2    Turner, R.J.3    Robinson, C.4
  • 104
    • 0036046656 scopus 로고    scopus 로고
    • Phospholipases C are involved in the virulence of Mycobacterium tuberculosis
    • Raynaud C, Guilhot C, Rauzier J, Bordat Y, Pelicic V, et al. 2002. Phospholipases C are involved in the virulence of Mycobacterium tuberculosis. Mol. Microbiol. 45:203-17
    • (2002) Mol. Microbiol. , vol.45 , pp. 203-217
    • Raynaud, C.1    Guilhot, C.2    Rauzier, J.3    Bordat, Y.4    Pelicic, V.5
  • 105
    • 30044442673 scopus 로고    scopus 로고
    • Targeting of unfolded PhoA to the Tat translocon of Escherichia coli
    • Richter S, Brüser T. 2005. Targeting of unfolded PhoA to the Tat translocon of Escherichia coli. J. Biol. Chem. 280:42723-30
    • (2005) J. Biol. Chem. , vol.280 , pp. 42723-42730
    • Richter, S.1    Brüser, T.2
  • 106
    • 0033532176 scopus 로고    scopus 로고
    • Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway
    • Rodrigue A, Chanal A, Beck K, Muller M, Wu LF. 1999. Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway. J. Biol. Chem. 274:13223-28
    • (1999) J. Biol. Chem. , vol.274 , pp. 13223-13228
    • Rodrigue, A.1    Chanal, A.2    Beck, K.3    Muller, M.4    Wu, L.F.5
  • 107
    • 0036038940 scopus 로고    scopus 로고
    • Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway
    • Rose RW, Brüser T, Kissinger JC, Pohlschroder M. 2002. Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway. Mol. Microbiol. 45:943-50
    • (2002) Mol. Microbiol. , vol.45 , pp. 943-950
    • Rose, R.W.1    Brüser, T.2    Kissinger, J.C.3    Pohlschroder, M.4
  • 108
    • 16244414601 scopus 로고    scopus 로고
    • The Legionella pneumophila tatB gene facilitates secretion of phospholipase C, growth under iron-limiting conditions, and intracellular infection
    • Rossier O, Cianciotto NP. 2005. The Legionella pneumophila tatB gene facilitates secretion of phospholipase C, growth under iron-limiting conditions, and intracellular infection. Infect. Immun. 73:2020-32
    • (2005) Infect. Immun. , vol.73 , pp. 2020-2032
    • Rossier, O.1    Cianciotto, N.P.2
  • 109
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: Watchdogs of the Escherichia coli cell envelope
    • Ruiz N, Silhavy TJ. 2005. Sensing external stress: watchdogs of the Escherichia coli cell envelope. Curr. Opin. Microbiol. 8:122-26
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 122-126
    • Ruiz, N.1    Silhavy, T.J.2
  • 110
    • 0034944416 scopus 로고    scopus 로고
    • Transport of cytochrome c derivatives by the bacterial Tat protein translocation system
    • Sanders C, Wethkamp N, Lill H. 2001. Transport of cytochrome c derivatives by the bacterial Tat protein translocation system. Mol. Microbiol. 41:241-46
    • (2001) Mol. Microbiol. , vol.41 , pp. 241-246
    • Sanders, C.1    Wethkamp, N.2    Lill, H.3
  • 111
    • 0035896573 scopus 로고    scopus 로고
    • Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock
    • Santini CL, Bernadac A, Zhang M, Chanal A, Ize B, et al. 2001. Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock. J. Biol. Chem. 276:8159-64
    • (2001) J. Biol. Chem. , vol.276 , pp. 8159-8164
    • Santini, C.L.1    Bernadac, A.2    Zhang, M.3    Chanal, A.4    Ize, B.5
  • 112
    • 0032472381 scopus 로고    scopus 로고
    • A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini CL, Ize B, Chanal A, Muller M, Giordano G, Wu LF. 1998. A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:101-12
    • (1998) EMBO J. , vol.17 , pp. 101-112
    • Santini, C.L.1    Ize, B.2    Chanal, A.3    Muller, M.4    Giordano, G.5    Wu, L.F.6
  • 114
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent F, Bogsch EG, Stanley NR, Wexler M, Robinson C, et al. 1998. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17:3640-50
    • (1998) EMBO J. , vol.17 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5
  • 115
    • 0034832014 scopus 로고    scopus 로고
    • Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure
    • Sargent F, Gohlke U, De Leeuw E, Stanley NR, Palmer T, et al. 2001. Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. Eur. J. Biochem. 268:3361-67
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3361-3367
    • Sargent, F.1    Gohlke, U.2    De Leeuw, E.3    Stanley, N.R.4    Palmer, T.5
  • 116
    • 0033579428 scopus 로고    scopus 로고
    • Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein
    • Sargent F, Stanley NR, Berks BC, Palmer T. 1999. Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein. J. Biol. Chem. 274:36073-82
    • (1999) J. Biol. Chem. , vol.274 , pp. 36073-36082
    • Sargent, F.1    Stanley, N.R.2    Berks, B.C.3    Palmer, T.4
  • 117
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti CM, Boyd DH, Rubin EJ. 2003. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 48:77-84
    • (2003) Mol. Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 118
    • 1642473932 scopus 로고    scopus 로고
    • The importance of the Tat-dependent protein secretion pathway in Streptomyces as revealed by phenotypic changes in tat deletion mutants and genome analysis
    • Schaerlaekens K, Van Mellaert L, Lammertyn E, Geukens N, Anne J. 2004. The importance of the Tat-dependent protein secretion pathway in Streptomyces as revealed by phenotypic changes in tat deletion mutants and genome analysis. Microbiology 150:21-31
    • (2004) Microbiology , vol.150 , pp. 21-31
    • Schaerlaekens, K.1    Van Mellaert, L.2    Lammertyn, E.3    Geukens, N.4    Anne, J.5
  • 119
    • 20444477153 scopus 로고    scopus 로고
    • Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane
    • Shimohata N, Akiyama Y, Ito K. 2005. Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane. J. Bacteriol. 187:3997-4004
    • (2005) J. Bacteriol. , vol.187 , pp. 3997-4004
    • Shimohata, N.1    Akiyama, Y.2    Ito, K.3
  • 120
  • 121
    • 0035190866 scopus 로고    scopus 로고
    • Escherichia coli strains blocked in Tat-dependent protein export exhibit pleiotropic defects in the cell envelope
    • Stanley NR, Findlay K, Berks BC, Palmer T. 2001. Escherichia coli strains blocked in Tat-dependent protein export exhibit pleiotropic defects in the cell envelope. J. Bacteriol. 183:139-44
    • (2001) J. Bacteriol. , vol.183 , pp. 139-144
    • Stanley, N.R.1    Findlay, K.2    Berks, B.C.3    Palmer, T.4
  • 122
    • 0034697156 scopus 로고    scopus 로고
    • The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli
    • Stanley NR, Palmer T, Berks BC. 2000. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 275:11591-96
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 123
    • 18844427294 scopus 로고    scopus 로고
    • Sec-dependent protein translocation across biological membranes: Evolutionary conservation of an essential protein transport pathway
    • review
    • Stephenson K. 2005. Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review). Mol. Membr. Biol. 22:17-28
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 17-28
    • Stephenson, K.1
  • 124
    • 0034604535 scopus 로고    scopus 로고
    • The thylakoid ΔpH-dependent pathway machinery facilitates RR-independent N-tail protein integration
    • Summer EJ, Mori H, Settles AM, Cline K. 2000. The thylakoid ΔpH-dependent pathway machinery facilitates RR-independent N-tail protein integration. J. Biol. Chem. 275:23483-90
    • (2000) J. Biol. Chem. , vol.275 , pp. 23483-23490
    • Summer, E.J.1    Mori, H.2    Settles, A.M.3    Cline, K.4
  • 125
    • 0035181362 scopus 로고    scopus 로고
    • Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli
    • Thomas JD, Daniel RA, Errington J, Robinson C. 2001. Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Mol. Microbiol. 39:47-53
    • (2001) Mol. Microbiol. , vol.39 , pp. 47-53
    • Thomas, J.D.1    Daniel, R.A.2    Errington, J.3    Robinson, C.4
  • 126
    • 19744375740 scopus 로고    scopus 로고
    • Characterization of fluorescent chimeras of cholera toxin and Escherichia coli heat-labile enterotoxins produced by use of the twin arginine translocation system
    • Tinker JK, Erbe JL, Holmes RK. 2005. Characterization of fluorescent chimeras of cholera toxin and Escherichia coli heat-labile enterotoxins produced by use of the twin arginine translocation system. Infect. Immun. 73:3627-35
    • (2005) Infect. Immun. , vol.73 , pp. 3627-3635
    • Tinker, J.K.1    Erbe, J.L.2    Holmes, R.K.3
  • 127
    • 0037317075 scopus 로고    scopus 로고
    • A novel protein fold and extreme domain swapping in the dimeric TorD chaperone from Shewanella massilia
    • Tranier S, Iobbi-Nivol C, Birck C, Ilbert M, Mortier-Barriere I, et al. 2003. A novel protein fold and extreme domain swapping in the dimeric TorD chaperone from Shewanella massilia. Structure 11:165-74
    • (2003) Structure , vol.11 , pp. 165-174
    • Tranier, S.1    Iobbi-Nivol, C.2    Birck, C.3    Ilbert, M.4    Mortier-Barriere, I.5
  • 128
    • 0036707997 scopus 로고    scopus 로고
    • Characterization and multiple molecular forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA
    • Tranier S, Mortier-Barriere I, Ilbert M, Birck C, Iobbi-Nivol C, et al. 2002. Characterization and multiple molecular forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA. Protein Sci. 11:2148-57
    • (2002) Protein Sci. , vol.11 , pp. 2148-2157
    • Tranier, S.1    Mortier-Barriere, I.2    Ilbert, M.3    Birck, C.4    Iobbi-Nivol, C.5
  • 129
    • 3142550604 scopus 로고    scopus 로고
    • Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)
    • Turner RJ, Papish AL, Sargent F. 2004. Sequence analysis of bacterial redox enzyme maturation proteins (REMPs). Can. J. Microbiol. 50:225-38
    • (2004) Can. J. Microbiol. , vol.50 , pp. 225-238
    • Turner, R.J.1    Papish, A.L.2    Sargent, F.3
  • 130
    • 0029566085 scopus 로고
    • Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli
    • Uchida K, Mori H, Mizushima S. 1995. Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 270:30862-68
    • (1995) J. Biol. Chem. , vol.270 , pp. 30862-30868
    • Uchida, K.1    Mori, H.2    Mizushima, S.3
  • 131
    • 0035803406 scopus 로고    scopus 로고
    • Involvement of the twin-arginine translocation system in protein secretion via the type II pathway
    • Voulhoux R, Ball G, Ize B, Vasil ML, Lazdunski A, et al. 2001. Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 20:6735-11
    • (2001) EMBO J. , vol.20 , pp. 6735-6811
    • Voulhoux, R.1    Ball, G.2    Ize, B.3    Vasil, M.L.4    Lazdunski, A.5
  • 132
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins
    • Weiner JH, Bilous PT, Shaw GM, Lubitz SP, Frost L, et al. 1998. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93:93-101
    • (1998) Cell , vol.93 , pp. 93-101
    • Weiner, J.H.1    Bilous, P.T.2    Shaw, G.M.3    Lubitz, S.P.4    Frost, L.5
  • 133
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • Wickner W, Schekman R. 2005. Protein translocation across biological membranes. Science 310:1452-56
    • (2005) Science , vol.310 , pp. 1452-1456
    • Wickner, W.1    Schekman, R.2
  • 134
    • 0035873543 scopus 로고    scopus 로고
    • Functional reconstitution of bacterial Tat translocation in vitro
    • Yahr TL, Wickner WT. 2001. Functional reconstitution of bacterial Tat translocation in vitro. EMBO J. 20:2472-79
    • (2001) EMBO J. , vol.20 , pp. 2472-2479
    • Yahr, T.L.1    Wickner, W.T.2
  • 135
    • 0036276602 scopus 로고    scopus 로고
    • Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system
    • Yen MR, Tseng YH, Nguyen EH, Wu LF, Saier MHJ. 2002. Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system. Arch. Microbiol. 177:441-50
    • (2002) Arch. Microbiol. , vol.177 , pp. 441-450
    • Yen, M.R.1    Tseng, Y.H.2    Nguyen, E.H.3    Wu, L.F.4    Saier, M.H.J.5
  • 136
    • 18844444516 scopus 로고    scopus 로고
    • Oxa1/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria (review)
    • Yi L, Dalbey RE. 2005. Oxa1/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria (review). Mol. Membr. Biol. 22:101-11
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 101-111
    • Yi, L.1    Dalbey, R.E.2
  • 137
    • 33750319466 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and how they get there
    • Scott JR, Barnett TC. 2006. Surface proteins of gram-positive bacteria and how they get there. Annu. Rev. Microbiol. 60: 397-423
    • (2006) Annu. Rev. Microbiol. , vol.60 , pp. 397-423
    • Scott, J.R.1    Barnett, T.C.2


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