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Volumn 12, Issue 4, 2003, Pages 937-946

Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CARRIER PROTEIN; SIGNAL PEPTIDE; TRANSACTIVATOR PROTEIN;

EID: 10744228022     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00398-8     Document Type: Article
Times cited : (265)

References (52)
  • 1
    • 0024566161 scopus 로고
    • In vitro membrane assembly of a polytopic, transmembrane protein results in an enzymatically active conformation
    • Ahrem B., Hoffschulte H.K., Müller M. In vitro membrane assembly of a polytopic, transmembrane protein results in an enzymatically active conformation. J. Cell Biol. 108:1989;1637-1646.
    • (1989) J. Cell Biol. , vol.108 , pp. 1637-1646
    • Ahrem, B.1    Hoffschulte, H.K.2    Müller, M.3
  • 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 L.F., Müller M. Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli. J. Biol. Chem. 277:2002;20499-20503.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20499-20503
    • Alami, M.1    Trescher, D.2    Wu, L.F.3    Müller, M.4
  • 3
    • 0037462475 scopus 로고    scopus 로고
    • Energetics of protein transport across biological membranes. A study of the thylakoid DeltapH-dependent/cpTat pathway
    • a
    • Alder N.N., Theg S.M. Energetics of protein transport across biological membranes. A study of the thylakoid DeltapH-dependent/cpTat pathway. Cell. 112:2003;231-242. a.
    • (2003) Cell , vol.112 , pp. 231-242
    • Alder, N.N.1    Theg, S.M.2
  • 4
    • 0037431011 scopus 로고    scopus 로고
    • Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport-incompetent substrate
    • b
    • Alder N.N., Theg S.M. Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport-incompetent substrate. FEBS Lett. 540:2003;96-100. b.
    • (2003) FEBS Lett. , vol.540 , pp. 96-100
    • Alder, N.N.1    Theg, S.M.2
  • 5
    • 0037155803 scopus 로고    scopus 로고
    • Essential cytoplasmic domains in the Escherichia coli TatC protein
    • Allen S.C., Barrett C.M., Ray N., Robinson C. Essential cytoplasmic domains in the Escherichia coli TatC protein. J. Biol. Chem. 277:2002;10362-10366.
    • (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 C.M., Mathers J.E., Robinson C. Identification of key regions within the Escherichia coli TatAB subunits. FEBS Lett. 537:2003;42-46.
    • (2003) FEBS Lett. , vol.537 , pp. 42-46
    • Barrett, C.M.1    Mathers, J.E.2    Robinson, C.3
  • 7
    • 0034602846 scopus 로고    scopus 로고
    • Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor
    • Beck K., Wu L.F., Brunner J., Müller M. Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor. EMBO J. 19:2000;134-143.
    • (2000) EMBO J. , vol.19 , pp. 134-143
    • Beck, K.1    Wu, L.F.2    Brunner, J.3    Müller, M.4
  • 8
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks B.C. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:1996;393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 11
    • 0030976930 scopus 로고    scopus 로고
    • Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein
    • Bogsch E., Brink S., Robinson C. Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein. EMBO J. 16:1997;3851-3859.
    • (1997) EMBO J. , vol.16 , pp. 3851-3859
    • Bogsch, E.1    Brink, S.2    Robinson, C.3
  • 12
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • Bogsch E.G., Sargent F., Stanley N.R., Berks B.C., Robinson C., Palmer T. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J. Biol. Chem. 273:1998;18003-18006.
    • (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
  • 13
    • 0034697250 scopus 로고    scopus 로고
    • Subunit interactions in the twin-arginine translocase complex of Escherichia coli
    • Bolhuis A., Bogsch E.G., Robinson C. Subunit interactions in the twin-arginine translocase complex of Escherichia coli. FEBS Lett. 472:2000;88-92.
    • (2000) FEBS Lett. , vol.472 , pp. 88-92
    • Bolhuis, A.1    Bogsch, E.G.2    Robinson, C.3
  • 14
    • 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 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. 276:2001;20213-20219.
    • (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
  • 15
    • 0142065248 scopus 로고    scopus 로고
    • Membrane targeting of a folded and cofactor-containing protein
    • Bruser T., Yano T., Brune D.C., Daldal F. Membrane targeting of a folded and cofactor-containing protein. Eur. J. Biochem. 270:2003;1211-1221.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1211-1221
    • Bruser, T.1    Yano, T.2    Brune, D.C.3    Daldal, F.4
  • 16
    • 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 B.C., Palmer T. 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. 177:2001;107-112.
    • (2001) Arch. Microbiol. , vol.177 , pp. 107-112
    • Buchanan, G.1    Sargent, F.2    Berks, B.C.3    Palmer, T.4
  • 17
    • 0036274596 scopus 로고    scopus 로고
    • Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis
    • Buchanan G., Leeuw E., Stanley N.R., Wexler M., Berks B.C., Sargent F., Palmer T. Functional complexity of the twin-arginine translocase TatC component revealed by site-directed mutagenesis. Mol. Microbiol. 43:2002;1457-1470.
    • (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    Sargent, F.6    Palmer, T.7
  • 18
    • 0000366608 scopus 로고
    • Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: In vivo probe for transcriptional control sequences
    • Casadaban M.J., Cohen S.N. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage. in vivo probe for transcriptional control sequences Proc. Natl. Acad. Sci. USA. 76:1979;4530-4533.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4530-4533
    • Casadaban, M.J.1    Cohen, S.N.2
  • 19
    • 0037470623 scopus 로고    scopus 로고
    • Specific inhibition of the translocation of a subset of Escherichia coli TAT substrates by the TorA signal peptide
    • Chanal A., Santini C.L., Wu L.F. Specific inhibition of the translocation of a subset of Escherichia coli TAT substrates by the TorA signal peptide. J. Mol. Biol. 327:2003;563-570.
    • (2003) J. Mol. Biol. , vol.327 , pp. 563-570
    • Chanal, A.1    Santini, C.L.2    Wu, L.F.3
  • 20
    • 0035920363 scopus 로고    scopus 로고
    • Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • Cline K., Mori H. Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J. Cell Biol. 154:2001;719-729.
    • (2001) J. Cell Biol. , vol.154 , pp. 719-729
    • Cline, K.1    Mori, H.2
  • 21
    • 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 B.C. Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. FEBS Lett. 506:2001;143-148.
    • (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
  • 23
    • 0037119435 scopus 로고    scopus 로고
    • Genetic analysis of the twin arginine translocator secretion pathway in bacteria
    • DeLisa M.P., Samuelson P., Palmer T., Georgiou G. Genetic analysis of the twin arginine translocator secretion pathway in bacteria. J. Biol. Chem. 277:2002;29825-29831.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29825-29831
    • DeLisa, M.P.1    Samuelson, P.2    Palmer, T.3    Georgiou, G.4
  • 24
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa M.P., Tullman D., Georgiou G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci. USA. 100:2003;6115-6120.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 25
    • 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 P.J. Agrobacterium tumefaciens twin-arginine-dependent translocation is important for virulence, flagellation, and chemotaxis but not type IV secretion. J. Bacteriol. 185:2003;760-771.
    • (2003) J. Bacteriol. , vol.185 , pp. 760-771
    • Ding, Z.1    Christie, P.J.2
  • 26
    • 0037450644 scopus 로고    scopus 로고
    • Thylakoid targeting of Tat passenger proteins shows no delta pH dependence in vivo
    • Finazzi G., Chasen C., Wollman F.A., de Vitry C. Thylakoid targeting of Tat passenger proteins shows no delta pH dependence in vivo. EMBO J. 22:2003;807-815.
    • (2003) EMBO J. , vol.22 , pp. 807-815
    • Finazzi, G.1    Chasen, C.2    Wollman, F.A.3    De Vitry, C.4
  • 27
    • 0037077710 scopus 로고    scopus 로고
    • Topology determination and functional analysis of the Escherichia coli TatC protein
    • Gouffi K., Santini C.L., Wu L.F. Topology determination and functional analysis of the Escherichia coli TatC protein. FEBS Lett. 525:2002;65-70.
    • (2002) FEBS Lett. , vol.525 , pp. 65-70
    • Gouffi, K.1    Santini, C.L.2    Wu, L.F.3
  • 28
    • 0037468635 scopus 로고    scopus 로고
    • The Escherichia coli twin-arginine translocase: Conserved residues of TatA and TatB family components involved in protein transport
    • Hicks M.G., de Leeuw E., Porcelli I., Buchanan G., Berks B.C., Palmer T. The Escherichia coli twin-arginine translocase. conserved residues of TatA and TatB family components involved in protein transport FEBS Lett. 539:2003;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
  • 29
    • 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 A.P., Stanley N.R., Palmer T., Berks B.C. A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif. FEBS Lett. 497:2001;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
  • 31
    • 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 R.L., Sargent F., Berks B.C., Sawers G., Palmer T. Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth. J. Bacteriol. 183:2001;1801-1804.
    • (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
  • 33
    • 0036837744 scopus 로고    scopus 로고
    • 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. 184:2002;5871-5879.
    • (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
  • 34
    • 0037092039 scopus 로고    scopus 로고
    • A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase
    • Mori H., Cline K. A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase. J. Cell Biol. 157:2002;205-210.
    • (2002) J. Cell Biol. , vol.157 , pp. 205-210
    • Mori, H.1    Cline, K.2
  • 35
    • 0035201578 scopus 로고    scopus 로고
    • Protein traffic in bacteria: Multiple routes from the ribosome to and across the membrane
    • Müller M., Koch H.G., Beck K., Schafer U. Protein traffic in bacteria. multiple routes from the ribosome to and across the membrane Prog. Nucleic Acid Res. Mol. Biol. 66:2001;107-157.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 107-157
    • Müller, M.1    Koch, H.G.2    Beck, K.3    Schafer, U.4
  • 37
    • 0037062507 scopus 로고    scopus 로고
    • Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis
    • Ochsner U.A., Snyder A., Vasil A.I., Vasil M.L. Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis. Proc. Natl. Acad. Sci. USA. 99:2002;8312-8317.
    • (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
  • 38
    • 0037352234 scopus 로고    scopus 로고
    • Moving folded proteins across the bacterial cell membrane
    • Palmer T., Berks B.C. Moving folded proteins across the bacterial cell membrane. Microbiol. 149:2003;547-556.
    • (2003) Microbiol. , vol.149 , pp. 547-556
    • Palmer, T.1    Berks, B.C.2
  • 40
    • 0035350689 scopus 로고    scopus 로고
    • Protein targeting by the twin-arginine translocation pathway
    • Robinson C., Bolhuis A. Protein targeting by the twin-arginine translocation pathway. Nat. Rev. Mol. Cell. Biol. 2:2001;350-356.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 350-356
    • Robinson, C.1    Bolhuis, A.2
  • 41
    • 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., Müller M., Wu L.F. Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway. J. Biol. Chem. 274:1999;13223-13228.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13223-13228
    • Rodrigue, A.1    Chanal, A.2    Beck, K.3    Müller, M.4    Wu, L.F.5
  • 42
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini C.L., Ize B., Chanal A., Müller M., Giordano G., Wu L.F. A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:1998;101-112.
    • (1998) EMBO J. , vol.17 , pp. 101-112
    • Santini, C.L.1    Ize, B.2    Chanal, A.3    Müller, M.4    Giordano, G.5    Wu, L.F.6
  • 43
    • 0032146314 scopus 로고    scopus 로고
    • Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit-identification of a soluble precursor of the small subunit in a hypB mutant
    • a
    • Sargent F., Ballantine S.P., Rugman P.A., Palmer T., Boxer D.H. Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit-identification of a soluble precursor of the small subunit in a hypB mutant. Eur. J. Biochem. 255:1998;746-754. a.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 746-754
    • Sargent, F.1    Ballantine, S.P.2    Rugman, P.A.3    Palmer, T.4    Boxer, D.H.5
  • 44
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • b
    • Sargent F., Bogsch E.G., Stanley N.R., Wexler M., Robinson C., Berks B.C., Palmer T. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17:1998;3640-3650. b.
    • (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    Berks, B.C.6    Palmer, T.7
  • 45
    • 0033579428 scopus 로고    scopus 로고
    • Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein
    • Sargent F., Stanley N.R., Berks B.C., Palmer T. Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein. J. Biol. Chem. 274:1999;36073-36082.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36073-36082
    • Sargent, F.1    Stanley, N.R.2    Berks, B.C.3    Palmer, T.4
  • 46
    • 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 N.R., Palmer T., Saibil H.R., Berks B.C. Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. Eur. J. Biochem. 268:2001;3361-3367.
    • (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    Saibil, H.R.6    Berks, B.C.7
  • 47
    • 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 N.R., Palmer T., Berks B.C. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 275:2000;11591-11596.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 49
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne G. The signal peptide. J. Membr. Biol. 115:1990;195-201.
    • (1990) J. Membr. Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 50
    • 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 M.L., Lazdunski A., Wu L.F., Filloux A. Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 20:2001;6735-6741.
    • (2001) EMBO J. , vol.20 , pp. 6735-6741
    • Voulhoux, R.1    Ball, G.2    Ize, B.3    Vasil, M.L.4    Lazdunski, A.5    Wu, L.F.6    Filloux, A.7
  • 52
    • 0035873543 scopus 로고    scopus 로고
    • Functional reconstitution of bacterial Tat translocation in vitro
    • Yahr T.L., Wickner W.T. Functional reconstitution of bacterial Tat translocation in vitro. EMBO J. 20:2001;2472-2479.
    • (2001) EMBO J. , vol.20 , pp. 2472-2479
    • Yahr, T.L.1    Wickner, W.T.2


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