메뉴 건너뛰기




Volumn 74, Issue 24, 2008, Pages 7507-7513

The twin-arginine signal peptide of Bacillus subtilis YwbN can direct either Tat- or Sec-dependent secretion of different cargo proteins: Secretion of active subtilisin via the B. subtilis Tat pathway

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; BACTERIOLOGY; ESCHERICHIA COLI; GENE ENCODING; PROTEINS; SUBSTRATES;

EID: 57449094805     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01401-08     Document Type: Article
Times cited : (38)

References (71)
  • 1
    • 41449118764 scopus 로고    scopus 로고
    • A minimal Tat system from a gram-positive organism: A bifunctional TatA subunit participates in discrete TatAC and TatA complexes
    • Barnett, J. P., R. T. Eijlander, O. P. Kuipers, and C. Robinson. 2008. A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes. J. Biol. Chem. 283:2534-2542.
    • (2008) J. Biol. Chem , vol.283 , pp. 2534-2542
    • Barnett, J.P.1    Eijlander, R.T.2    Kuipers, O.P.3    Robinson, C.4
  • 2
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B. 1996. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:12.
    • (1996) Mol. Microbiol , vol.22 , pp. 12
    • Berks, B.1
  • 4
    • 0037407866 scopus 로고    scopus 로고
    • Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane
    • Blaudeck, N., P. Kreutzenbeck, R. Freudl, and G. A. Sprenger. 2003. Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane. J. Bacteriol. 185:2811-2819.
    • (2003) J. Bacteriol , vol.185 , pp. 2811-2819
    • Blaudeck, N.1    Kreutzenbeck, P.2    Freudl, R.3    Sprenger, G.A.4
  • 5
    • 0030976930 scopus 로고    scopus 로고
    • Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Secavoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein
    • Bogsch, E., S. Brink, and C. Robinson. 1997. Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Secavoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein. EMBO J. 16:3851-3859.
    • (1997) EMBO J , vol.16 , pp. 3851-3859
    • Bogsch, E.1    Brink, S.2    Robinson, C.3
  • 6
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • Bogsch, E. G., F. Sargent, N. R. Stanley, B. C. Berks, C. Robinson, and T. Palmer. 1998. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J. Biol. Chem. 273: 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
  • 8
    • 0344457370 scopus 로고    scopus 로고
    • Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli
    • Bron, S., A. Bolhuis, H. Tjalsma, S. Holsappel, G. Venema, and J. M. van Dijl. 1998. Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli. J. Biotechnol. 64:3-13.
    • (1998) J. Biotechnol , vol.64 , pp. 3-13
    • Bron, S.1    Bolhuis, A.2    Tjalsma, H.3    Holsappel, S.4    Venema, G.5    van Dijl, J.M.6
  • 9
    • 0015335342 scopus 로고
    • Ultraviolet inactivation and excision-repair in Bacillus subtilis. I. Construction and characterization of a transformable eightfold auxotrophic strain and two ultraviolet-sensitive derivatives
    • Bron, S., and G. Venema. 1972. Ultraviolet inactivation and excision-repair in Bacillus subtilis. I. Construction and characterization of a transformable eightfold auxotrophic strain and two ultraviolet-sensitive derivatives. Mutat. Res. 15:1-10.
    • (1972) Mutat. Res , vol.15 , pp. 1-10
    • Bron, S.1    Venema, G.2
  • 10
    • 0028945041 scopus 로고
    • A monomeric, tightly folded stromal intermediate on the delta pH-dependent thylakoidal protein transport pathway
    • Creighton, A. M., A. Hulford, A. Mant, D. Robinson, and C. Robinson. 1995. A monomeric, tightly folded stromal intermediate on the delta pH-dependent thylakoidal protein transport pathway. J. Biol. Chem. 270:1663-1669.
    • (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
  • 11
    • 0040537042 scopus 로고    scopus 로고
    • Competition between Sec- and TAT-dependent protein translocation in Escherichia coli
    • Cristobal, S., J. W. de Gier, H. Nielsen, and G. von Heijne. 1999. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 18:2982-2990.
    • (1999) EMBO J , vol.18 , pp. 2982-2990
    • Cristobal, S.1    de Gier, J.W.2    Nielsen, H.3    von Heijne, G.4
  • 13
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa, M. P., D. Tullman, and G. Georgiou. 2003. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci. USA 100:6115-6120.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 14
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in Escherichia coli
    • Feilmeier, B. J., G. Iseminger, D. Schroeder, H. Webber, and G. J. Phillips. 2000. Green fluorescent protein functions as a reporter for protein localization in Escherichia coli. J. Bacteriol. 182:4068-4076.
    • (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
  • 15
    • 0001949658 scopus 로고
    • Commercial production of extracellular enzymes
    • A. L. Sonenshein, J. A. Hoch, and R. Losick ed, American Society for Microbiology, Washington, DC
    • Ferrari, E., A. S. Jarnagin, and B. F. Schmidt. 1993. Commercial production of extracellular enzymes, p. 917-937. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria. American Society for Microbiology, Washington, DC.
    • (1993) Bacillus subtilis and other gram-positive bacteria , pp. 917-937
    • Ferrari, E.1    Jarnagin, A.S.2    Schmidt, B.F.3
  • 16
    • 6344235275 scopus 로고    scopus 로고
    • Tat dependent export of E. coli phytase AppA by using the PhoD-specific transport system of Bacillus subtilis
    • Gerlach, R., O. Pop, and J. P. Muller. 2004. Tat dependent export of E. coli phytase AppA by using the PhoD-specific transport system of Bacillus subtilis. J. Basic Microbiol. 44:351-359.
    • (2004) J. Basic Microbiol , vol.44 , pp. 351-359
    • Gerlach, R.1    Pop, O.2    Muller, J.P.3
  • 18
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • Guerout-Fleury, A. M., K. Shazand, N. Frandsen, and P. Stragier. 1995. Antibiotic-resistance cassettes for Bacillus subtilis. Gene 167:335-336.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guerout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 19
    • 0026752273 scopus 로고
    • Bacillus subtilis and its relatives: Molecular biological and industrial workhorses
    • Harwood, C. R. 1992. Bacillus subtilis and its relatives: molecular biological and industrial workhorses. Trends Biotechnol. 10:247-256.
    • (1992) Trends Biotechnol , vol.10 , pp. 247-256
    • Harwood, C.R.1
  • 20
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: An unfolding story
    • Harwood, C. R., and R. Cranenburgh. 2008. Bacillus protein secretion: an unfolding story. Trends Microbiol. 16:73-79.
    • (2008) Trends Microbiol , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 21
    • 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., N. R. Stanley, T. Palmer, and B. C. Berks. 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
  • 22
    • 0032567332 scopus 로고    scopus 로고
    • The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane
    • Hynds, P. J., D. Robinson, and C. Robinson. 1998. The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane. J. Biol. Chem. 273:34868-34874.
    • (1998) J. Biol. Chem , vol.273 , pp. 34868-34874
    • Hynds, P.J.1    Robinson, D.2    Robinson, C.3
  • 23
    • 0026324509 scopus 로고
    • Intramolecular chaperone: The role of the pro-peptide in protein folding
    • Inouye, M. 1991. Intramolecular chaperone: the role of the pro-peptide in protein folding. Enzyme 45:314-321.
    • (1991) Enzyme , vol.45 , pp. 314-321
    • Inouye, M.1
  • 24
    • 0036431451 scopus 로고    scopus 로고
    • In vivo assessment of the Tat signal peptide specificity in Escherichia coli
    • Ize, B., F. Gerard, and L. F. Wu. 2002. In vivo assessment of the Tat signal peptide specificity in Escherichia coli. Arch. Microbiol. 178:548-553.
    • (2002) Arch. Microbiol , vol.178 , pp. 548-553
    • Ize, B.1    Gerard, F.2    Wu, L.F.3
  • 28
    • 30344440093 scopus 로고    scopus 로고
    • Bifunctional TatA subunits in minimal Tat protein translocases
    • Jongbloed, J. D., R. van der Ploeg, and J. M. van Dijl. 2006. Bifunctional TatA subunits in minimal Tat protein translocases. Trends Microbiol. 14:2-4.
    • (2006) Trends Microbiol , vol.14 , pp. 2-4
    • Jongbloed, J.D.1    van der Ploeg, R.2    van Dijl, J.M.3
  • 30
    • 0027222723 scopus 로고
    • The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion
    • Kontinen, V. P., and M. Sarvas. 1993. The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion. Mol. Microbiol. 8:727-737.
    • (1993) Mol. Microbiol , vol.8 , pp. 727-737
    • Kontinen, V.P.1    Sarvas, M.2
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 33645365498 scopus 로고    scopus 로고
    • Coexpression of TorD enhances the transport of GFP via the TAT pathway
    • Li, S. Y., B. Y. Chang, and S. C. Lin. 2006. Coexpression of TorD enhances the transport of GFP via the TAT pathway. J. Biotechnol. 122:412-421.
    • (2006) J. Biotechnol , vol.122 , pp. 412-421
    • Li, S.Y.1    Chang, B.Y.2    Lin, S.C.3
  • 35
    • 0036456146 scopus 로고    scopus 로고
    • Bacillus subtilis functional genomics: Genome-wide analysis of the DegS-DegU regulon by transcriptomics and proteomics
    • Mader, U., H. Antelmann, T. Buder, M. K. Dahl, M. Hecker, and G. Homuth. 2002. Bacillus subtilis functional genomics: genome-wide analysis of the DegS-DegU regulon by transcriptomics and proteomics. Mol. Genet. Genomics 268:455-467.
    • (2002) Mol. Genet. Genomics , vol.268 , pp. 455-467
    • Mader, U.1    Antelmann, H.2    Buder, T.3    Dahl, M.K.4    Hecker, M.5    Homuth, G.6
  • 37
    • 34548019942 scopus 로고    scopus 로고
    • Comparative analysis of twin-arginine (Tat)-dependent protein secretion of a heterologous model protein (GFP) in three different Gram-positive bacteria
    • Meissner, D., A. Vollstedt, J. M. van Dijl, and R. Freudl. 2007. Comparative analysis of twin-arginine (Tat)-dependent protein secretion of a heterologous model protein (GFP) in three different Gram-positive bacteria. Appl. Microbiol. Biotechnol. 76:633-642.
    • (2007) Appl. Microbiol. Biotechnol , vol.76 , pp. 633-642
    • Meissner, D.1    Vollstedt, A.2    van Dijl, J.M.3    Freudl, R.4
  • 38
    • 37349039720 scopus 로고    scopus 로고
    • The Escherichia coli TatABC system and a Bacillus subtilis TatAC-type system recognise three distinct targeting determinants in twin-arginine signal peptides
    • Mendel, S., A. McCarthy, J. P. Barnett, R. T. Eijlander, O. P. Kuipers, and C. Robinson. 2008. The Escherichia coli TatABC system and a Bacillus subtilis TatAC-type system recognise three distinct targeting determinants in twin-arginine signal peptides. J. Mol. Biol. 375:661-672.
    • (2008) J. Mol. Biol , vol.375 , pp. 661-672
    • Mendel, S.1    McCarthy, A.2    Barnett, J.P.3    Eijlander, R.T.4    Kuipers, O.P.5    Robinson, C.6
  • 39
    • 50049087513 scopus 로고    scopus 로고
    • Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-distinct translocases and mechanisms
    • Natale, P., T. Bruser, and A. J. Driessen. 2008. Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-distinct translocases and mechanisms. Biochim. Biophys. Acta 1778:1735-1756.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1735-1756
    • Natale, P.1    Bruser, T.2    Driessen, A.J.3
  • 40
    • 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., C. M. Barrett, J. P. Barnett, K. G. Byrne, A. Bolhuis, and C. Robinson. 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
  • 41
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik, I. J., C. L. Ladner, and R. J. Turner. 2001. Identification of a twin-arginine leader-binding protein. Mol. Microbiol. 40:323-331.
    • (2001) Mol. Microbiol , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 42
    • 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, A. L., C. L. Ladner, and R. J. Turner. 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. 278:32501-32506.
    • (2003) J. Biol. Chem , vol.278 , pp. 32501-32506
    • Papish, A.L.1    Ladner, C.L.2    Turner, R.J.3
  • 43
    • 33847396185 scopus 로고    scopus 로고
    • An essential role for the DnaK molecular chaperone in stabilizing over-expressed substrate proteins of the bacterial twin-arginine translocation pathway
    • Perez-Rodriguez, R., A. C. Fisher, J. D. Perlmutter, M. G. Hicks, A. Chanal, C. L. Santini, L. F. Wu, T. Palmer, and M. P. DeLisa. 2007. An essential role for the DnaK molecular chaperone in stabilizing over-expressed substrate proteins of the bacterial twin-arginine translocation pathway. J. Mol. Biol. 367:715-730.
    • (2007) J. Mol. Biol , vol.367 , pp. 715-730
    • Perez-Rodriguez, R.1    Fisher, A.C.2    Perlmutter, J.D.3    Hicks, M.G.4    Chanal, A.5    Santini, C.L.6    Wu, L.F.7    Palmer, T.8    DeLisa, M.P.9
  • 44
    • 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., U. Martin, C. Abel, and J. P. Muller. 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. 277:3268-3273.
    • (2002) J. Biol. Chem , vol.277 , pp. 3268-3273
    • Pop, O.1    Martin, U.2    Abel, C.3    Muller, J.P.4
  • 45
    • 41149137584 scopus 로고    scopus 로고
    • The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway
    • Qiu, Y., R. Zhang, T. A. Binkowski, V. Tereshko, A. Joachimiak, and A. Kossiakoff. 2008. The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway. Proteins 71:525-533.
    • (2008) Proteins , vol.71 , pp. 525-533
    • Qiu, Y.1    Zhang, R.2    Binkowski, T.A.3    Tereshko, V.4    Joachimiak, A.5    Kossiakoff, A.6
  • 46
    • 36348950408 scopus 로고    scopus 로고
    • Functional tat transport of unstructured, small, hydrophilic proteins
    • Richter, S., U. Lindenstrauss, C. Lucke, R. Bayliss, and T. Bruser. 2007. Functional tat transport of unstructured, small, hydrophilic proteins. J. Biol. Chem. 282:33257-33264.
    • (2007) J. Biol. Chem , vol.282 , pp. 33257-33264
    • Richter, S.1    Lindenstrauss, U.2    Lucke, C.3    Bayliss, R.4    Bruser, T.5
  • 47
    • 0034012712 scopus 로고    scopus 로고
    • The twin-arginine translocation system: A novel means of transporting folded proteins in chloroplasts and bacteria
    • Robinson, C. 2000. The twin-arginine translocation system: a novel means of transporting folded proteins in chloroplasts and bacteria. Biol. Chem. 381:89-93.
    • (2000) Biol. Chem , vol.381 , pp. 89-93
    • Robinson, C.1
  • 48
    • 0035350689 scopus 로고    scopus 로고
    • Protein targeting by the twin-arginine translocation pathway
    • Robinson, C., and A. Bolhuis. 2001. Protein targeting by the twin-arginine translocation pathway. Nat. Rev. Mol. Cell Biol. 2:350-356.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 350-356
    • Robinson, C.1    Bolhuis, A.2
  • 49
    • 8844280791 scopus 로고    scopus 로고
    • Tat-dependent protein targeting in prokaryotes and chloroplasts
    • Robinson, C., and A. Bolhuis. 2004. Tat-dependent protein targeting in prokaryotes and chloroplasts. Biochim. Biophys. Acta 1694:135-147.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 135-147
    • Robinson, C.1    Bolhuis, A.2
  • 51
    • 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, C. L., A. Bernadac, M. Zhang, A. Chanal, B. Ize, C. Blanco, and L. F. Wu. 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. 276:8159-8164.
    • (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    Blanco, C.6    Wu, L.F.7
  • 52
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • Santini, C. L., B. Ize, A. Chanal, M. Muller, G. Giordano, and L. F. Wu. 1998. A novel sec-independent periplasmic protein translocation pathway in Escherichia coli. EMBO J. 17:101-112.
    • (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
  • 53
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: Moving folded proteins across membranes
    • Sargent, F. 2007. The twin-arginine transport system: moving folded proteins across membranes. Biochem. Soc Trans. 35:835-847.
    • (2007) Biochem. Soc Trans , vol.35 , pp. 835-847
    • Sargent, F.1
  • 54
    • 0036311769 scopus 로고    scopus 로고
    • Assembly of membrane-bound respiratory complexes by the Tat protein-transport system
    • Sargent, F., B. C. Berks, and T. Palmer. 2002. Assembly of membrane-bound respiratory complexes by the Tat protein-transport system. Arch. Microbiol. 178:77-84.
    • (2002) Arch. Microbiol , vol.178 , pp. 77-84
    • Sargent, F.1    Berks, B.C.2    Palmer, T.3
  • 55
    • 33644856642 scopus 로고    scopus 로고
    • Pathfinders and trailblazers: A prokaryotic targeting system for transport of folded proteins
    • Sargent, F., B. C. Berks, and T. Palmer. 2006. Pathfinders and trailblazers: a prokaryotic targeting system for transport of folded proteins. FEMS Microbiol. Lett. 254:198-207.
    • (2006) FEMS Microbiol. Lett , vol.254 , pp. 198-207
    • Sargent, F.1    Berks, B.C.2    Palmer, T.3
  • 56
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent, F., E. G. Bogsch, N. R. Stanley, M. Wexler, C. Robinson, B. C. Berks, and T. Palmer. 1998. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17:3640-3650.
    • (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
  • 57
    • 8844264456 scopus 로고    scopus 로고
    • Post-translocational folding of secretory proteins in Gram-positive bacteria
    • Sarvas, M., C. R. Harwood, S. Bron, and J. M. van Dijl. 2004. Post-translocational folding of secretory proteins in Gram-positive bacteria. Biochim. Biophys. Acta 1694:311-327.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 311-327
    • Sarvas, M.1    Harwood, C.R.2    Bron, S.3    van Dijl, J.M.4
  • 58
    • 1942538348 scopus 로고    scopus 로고
    • Developments in the use of Bacillus species for industrial production
    • Schallmey, M., A. Singh, and O. P. Ward. 2004. Developments in the use of Bacillus species for industrial production. Can. J. Microbiol. 50:1-17.
    • (2004) Can. J. Microbiol , vol.50 , pp. 1-17
    • Schallmey, M.1    Singh, A.2    Ward, O.P.3
  • 59
    • 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., T. Palmer, and B. C. Berks. 2000. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 275:11591-11596.
    • (2000) J. Biol. Chem , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 60
    • 0032479216 scopus 로고    scopus 로고
    • The influence of protein folding on late stages of the secretion of alpha-amylases from Bacillus subtilis
    • Stephenson, K., N. M. Carter, C. R. Harwood, M. F. Petit-Glatron, and R. Chambert. 1998. The influence of protein folding on late stages of the secretion of alpha-amylases from Bacillus subtilis. FEBS Lett. 430:385-389.
    • (1998) FEBS Lett , vol.430 , pp. 385-389
    • Stephenson, K.1    Carter, N.M.2    Harwood, C.R.3    Petit-Glatron, M.F.4    Chambert, R.5
  • 61
    • 0034663718 scopus 로고    scopus 로고
    • The influence of secretory-protein charge on late stages of secretion from the Gram-positive bacterium Bacillus subtilis
    • Stephenson, K., C. L. Jensen, S. T. Jorgensen, J. H. Lakey, and C. R. Harwood. 2000. The influence of secretory-protein charge on late stages of secretion from the Gram-positive bacterium Bacillus subtilis. Biochem. J. 350:31-39.
    • (2000) Biochem. J , vol.350 , pp. 31-39
    • Stephenson, K.1    Jensen, C.L.2    Jorgensen, S.T.3    Lakey, J.H.4    Harwood, C.R.5
  • 62
    • 0033231926 scopus 로고    scopus 로고
    • How to get a folded protein across a membrane
    • Teter, S. A., and D. J. Klionsky. 1999. How to get a folded protein across a membrane. Trends Cell Biol. 9:428-431.
    • (1999) Trends Cell Biol , vol.9 , pp. 428-431
    • Teter, S.A.1    Klionsky, D.J.2
  • 63
    • 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, J. D., R. A. Daniel, J. Errington, and C. Robinson. 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
  • 65
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma, H., A. Bolhuis, J. D. Jongbloed, S. Bron, and J. M. van Dijl. 2000. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 64:515-547.
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    van Dijl, J.M.5
  • 68
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins
    • Weiner, J. H., P. T. Bilous, G. M. Shaw, S. P. Lubitz, L. Frost, G. H. Thomas, J. A. Cole, and R. J. Turner. 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    Thomas, G.H.6    Cole, J.A.7    Turner, R.J.8
  • 70
    • 37349115561 scopus 로고    scopus 로고
    • A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life
    • Widdick, D. A., R. T. Eijlander, J. M. van Dijl, O. P. Kuipers, and T. Palmer. 2008. A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life. J. Mol. Biol. 375:595-603.
    • (2008) J. Mol. Biol , vol.375 , pp. 595-603
    • Widdick, D.A.1    Eijlander, R.T.2    van Dijl, J.M.3    Kuipers, O.P.4    Palmer, T.5
  • 71
    • 57449117206 scopus 로고    scopus 로고
    • 2nd ed. CRC Press, Boca Raton, FL
    • Zeigler, D. R., and J. B. Perkins. 2008. Bacillus, 2nd ed. CRC Press, Boca Raton, FL.
    • (2008) Bacillus
    • Zeigler, D.R.1    Perkins, J.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.