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Volumn 1, Issue 5, 2008, Pages 403-415

Exploration of twin-arginine translocation for expression and purification of correctly folded proteins in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL PROTEIN; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; SIGNAL PEPTIDE;

EID: 62649170149     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2008.00041.x     Document Type: Article
Times cited : (27)

References (69)
  • 1
    • 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., and Muller, M. (2002) Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli. J Biol Chem 277: 20499-20503.
    • (2002) J Biol Chem , vol.277 , pp. 20499-20503
    • Alami, M.1    Trescher, D.2    Wu, L.F.3    Muller, M.4
  • 2
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single - chain antibodies
    • Bach, H., Mazor, Y., Shaky, S., Shoham-Lev, A., Berdichevsky, Y., Gutnick, D.L., and Benhar, I. (2001) Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single - chain antibodies. J Mol Biol 312: 79-93.
    • (2001) J Mol Biol , vol.312 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3    Shoham-Lev, A.4    Berdichevsky, Y.5    Gutnick, D.L.6    Benhar, I.7
  • 3
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx, F. (1999) Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol 10: 411-421.
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 4
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx, F., and Mujacic, M. (2004) Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 22: 1399-1408.
    • (2004) Nat Biotechnol , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 5
    • 0037414423 scopus 로고    scopus 로고
    • Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli
    • Barrett, C.M., Ray, N., Thomas, J.D., Robinson, C., and Bolhuis, A. (2003) Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli. Biochem Biophys Res Commun 304: 279-284.
    • (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
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B.C. (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
  • 9
    • 0034663493 scopus 로고    scopus 로고
    • A novel protein transport system involved in the biogenesis of bacterial electron transfer chains
    • Berks, B.C., Sargent, F., De Leeuw, E., Hinsley, A.P., Stanley, N.R., Jack, R.L., et al. (2000a) A novel protein transport system involved in the biogenesis of bacterial electron transfer chains. Biochim Biophys Acta 1459: 325-330.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 325-330
    • Berks, B.C.1    Sargent, F.2    De Leeuw, E.3    Hinsley, A.P.4    Stanley, N.R.5    Jack, R.L.6
  • 10
  • 11
    • 0141672034 scopus 로고    scopus 로고
    • The Tat protein translocation pathway and its role in microbial physiology
    • Berks, B.C., Palmer, T., and 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
  • 12
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette, P.H., Aslund, F., Beckwith, J., and Georgiou, G. (1999) Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc Natl Acad Sci USA 96: 13703-13708.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 13
    • 0035150176 scopus 로고    scopus 로고
    • Specificity of signal peptide recognition in tatdependent bacterial protein translocation
    • Blaudeck, N., Sprenger, G.A., Freudl, R., and Wiegert, T. (2001) Specificity of signal peptide recognition in tatdependent bacterial protein translocation. J Bacteriol 183: 604-610.
    • (2001) J Bacteriol , vol.183 , pp. 604-610
    • Blaudeck, N.1    Sprenger, G.A.2    Freudl, R.3    Wiegert, T.4
  • 14
    • 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., and Sprenger, G.A. (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
  • 15
    • 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., and Palmer, T. (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
  • 16
    • 34547569679 scopus 로고    scopus 로고
    • The twin-arginine translocation system and its capability for protein secretion in biotechnological protein production
    • Bruser, T. (2007) The twin-arginine translocation system and its capability for protein secretion in biotechnological protein production. Appl Microbiol Biotechnol 76: 35-45.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 35-45
    • Bruser, T.1
  • 17
    • 0142065248 scopus 로고    scopus 로고
    • Membrane targeting of a folded and cofactor-containing protein
    • Bruser, T., Yano, T., Brune, D.C., and Daldal, F. (2003) Membrane targeting of a folded and cofactor-containing protein. Eur J Biochem 270: 1211-1221.
    • (2003) Eur J Biochem , vol.270 , pp. 1211-1221
    • Bruser, T.1    Yano, T.2    Brune, D.C.3    Daldal, F.4
  • 18
    • 0035014528 scopus 로고    scopus 로고
    • Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS)
    • Chen, G., Hayhurst, A., Thomas, J.G., Harvey, B.R., Iverson, B.L., and Georgiou, G. (2001) Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS). Nat Biotechnol 19: 537-542.
    • (2001) Nat Biotechnol , vol.19 , pp. 537-542
    • Chen, G.1    Hayhurst, A.2    Thomas, J.G.3    Harvey, B.R.4    Iverson, B.L.5    Georgiou, G.6
  • 19
    • 34447307436 scopus 로고    scopus 로고
    • Evidence for a dynamic and transient pathway through the TAT protein transport machinery
    • Cline, K., and McCaffery, M. (2007) Evidence for a dynamic and transient pathway through the TAT protein transport machinery. EMBO J 26: 3039-3049.
    • (2007) EMBO J , vol.26 , pp. 3039-3049
    • Cline, K.1    McCaffery, M.2
  • 20
    • 0037119435 scopus 로고    scopus 로고
    • Genetic analysis of the twin arginine translocator secretion pathway in bacteria
    • DeLisa, M.P., Samuelson, P., Palmer, T., and Georgiou, G. (2002) Genetic analysis of the twin arginine translocator secretion pathway in bacteria. J Biol Chem 277: 29825-29831.
    • (2002) J Biol Chem , vol.277 , pp. 29825-29831
    • DeLisa, M.P.1    Samuelson, P.2    Palmer, T.3    Georgiou, G.4
  • 21
    • 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., and Georgiou, G. (2003) Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc Natl Acad Sci USA 100: 6115-6120.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 22
    • 0346655242 scopus 로고    scopus 로고
    • Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway
    • DeLisa, M.P., Lee, P., Palmer, T., and Georgiou, G. (2004) Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway. J Bacteriol 186: 366-373.
    • (2004) J Bacteriol , vol.186 , pp. 366-373
    • DeLisa, M.P.1    Lee, P.2    Palmer, T.3    Georgiou, G.4
  • 23
    • 0035852860 scopus 로고    scopus 로고
    • Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries
    • Dekker, N., Cox, R.C., Kramer, R.A., and Egmond, M.R. (2001) Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries. Biochemistry 40: 1694-1701.
    • (2001) Biochemistry , vol.40 , pp. 1694-1701
    • Dekker, N.1    Cox, R.C.2    Kramer, R.A.3    Egmond, M.R.4
  • 24
    • 0029017155 scopus 로고
    • Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: A caution for gene fusion studies
    • Derman, A.I., and Beckwith, J. (1995) Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: a caution for gene fusion studies. J Bacteriol 177: 3764-3770.
    • (1995) J Bacteriol , vol.177 , pp. 3764-3770
    • Derman, A.I.1    Beckwith, J.2
  • 25
    • 0027457077 scopus 로고
    • A signal sequence is not required for protein export in prlA mutants of Escherichia coli
    • Derman, A.I., Puziss, J.W., Bassford, P.J., Jr., and Beckwith, J. (1993) A signal sequence is not required for protein export in prlA mutants of Escherichia coli. EMBO J 12: 879-888.
    • (1993) EMBO J , vol.12 , pp. 879-888
    • Derman, A.I.1    Puziss, J.W.2    Bassford Jr., P.J.3    Beckwith, J.4
  • 26
    • 0037317124 scopus 로고    scopus 로고
    • Prokaryotic utilization of the twin-arginine translocation pathway: A genomic survey
    • Dilks, K., Rose, R.W., Hartmann, E., and Pohlschroder, M. (2003) Prokaryotic utilization of the twin-arginine translocation pathway: a genomic survey. J Bacteriol 185: 1478-1483.
    • (2003) J Bacteriol , vol.185 , pp. 1478-1483
    • Dilks, K.1    Rose, R.W.2    Hartmann, E.3    Pohlschroder, M.4
  • 27
    • 0034995184 scopus 로고    scopus 로고
    • The structural basis of protein targeting and translocation in bacteria
    • Driessen, A.J., Manting, E.H., and van der Does, C. (2001) The structural basis of protein targeting and translocation in bacteria. Nat Struct Biol 8: 492-498.
    • (2001) Nat Struct Biol , vol.8 , pp. 492-498
    • Driessen, A.J.1    Manting, E.H.2    van der Does, C.3
  • 28
    • 0033917124 scopus 로고    scopus 로고
    • Green fluorescent protein functions as a reporter for protein localization in Escherichia coli
    • Feilmeier, B.J., Iseminger, G., Schroeder, D., Webber, H., and Phillips, G.J. (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
  • 29
    • 0025216609 scopus 로고    scopus 로고
    • Fikes, J.D., Barkocy-Gallagher, G.A., Klapper, D.G., and Bassford, P.J., Jr. (1990) Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site. J Biol Chem 265: 3417-3423.
    • Fikes, J.D., Barkocy-Gallagher, G.A., Klapper, D.G., and Bassford, P.J., Jr. (1990) Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site. J Biol Chem 265: 3417-3423.
  • 30
    • 33644536727 scopus 로고    scopus 로고
    • Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway
    • Fisher, A.C., Kim,W., and DeLisa, M.P. (2006) Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway. Protein Sci 15: 449-458.
    • (2006) Protein Sci , vol.15 , pp. 449-458
    • Fisher, A.C.1    Kim, W.2    DeLisa, M.P.3
  • 31
    • 0027425230 scopus 로고
    • Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface
    • Francisco, J.A., Campbell, R., Iverson, B.L., and 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: 10444-10448.
    • (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
  • 32
    • 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., and 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: 3085-3092.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3085-3092
    • Gauthier, C.1    Li, H.2    Morosoli, R.3
  • 34
    • 0023916082 scopus 로고
    • Association of degradation and secretion of three chimeric polypeptides in Escherichia coli
    • Gentz, R., Kuys, Y., Zwieb, C., Taatjes, D., Taatjes, H., Bannwarth, W., et al. (1988) Association of degradation and secretion of three chimeric polypeptides in Escherichia coli. J Bacteriol 170: 2212-2220.
    • (1988) J Bacteriol , vol.170 , pp. 2212-2220
    • Gentz, R.1    Kuys, Y.2    Zwieb, C.3    Taatjes, D.4    Taatjes, H.5    Bannwarth, W.6
  • 35
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: Status report and future prospects
    • Georgiou, G., and Segatori, L. (2005) Preparative expression of secreted proteins in bacteria: status report and future prospects. Curr Opin Biotechnol 16: 538-545.
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 36
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • di Guan, C., Li, P., Riggs, P.D., and Inouye, H. (1988) Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67: 21-30.
    • (1988) Gene , vol.67 , pp. 21-30
    • di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 37
    • 3042647616 scopus 로고    scopus 로고
    • Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries
    • Harvey, B.R., Georgiou, G., Hayhurst, A., Jeong, K.J., Iverson, B.L., and Rogers, G.K. (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: 9193-9198.
    • (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
  • 38
    • 0035629780 scopus 로고    scopus 로고
    • High-throughput antibody isolation
    • Hayhurst, A., and Georgiou, G. (2001) High-throughput antibody isolation. Curr Opin Chem Biol 5: 683-689.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 683-689
    • Hayhurst, A.1    Georgiou, G.2
  • 39
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust, R.B., and Waugh, D.S. (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8: 1668-1674.
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 40
    • 0021215684 scopus 로고
    • Mutation prlF1 relieves the lethality associated with export of beta-galactosidase hybrid proteins in Escherichia coli
    • Kiino, D.R., and Silhavy, T.J. (1984) Mutation prlF1 relieves the lethality associated with export of beta-galactosidase hybrid proteins in Escherichia coli. J Bacteriol 158: 878-883.
    • (1984) J Bacteriol , vol.158 , pp. 878-883
    • Kiino, D.R.1    Silhavy, T.J.2
  • 41
    • 29144447051 scopus 로고    scopus 로고
    • Twin-arginine translocation of active human tissue plasminogen activator in Escherichia coli
    • Kim, J.-Y., Fogarty, E.A., Lu, F.J., Zhu, H., Henderson, L.A., and DeLisa, M.P. (2005) Twin-arginine translocation of active human tissue plasminogen activator in Escherichia coli. Appl Environ Microbiol 71: 8451-8459.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8451-8459
    • Kim, J.-Y.1    Fogarty, E.A.2    Lu, F.J.3    Zhu, H.4    Henderson, L.A.5    DeLisa, M.P.6
  • 42
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomic-level accuracy
    • Kuhlman, B., Dantas, G., Ireton, G.C., Varani, G., Stoddard, B.L., and Baker, D. (2003) Design of a novel globular protein fold with atomic-level accuracy. Science 302: 1364-1368.
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard, B.L.5    Baker, D.6
  • 43
    • 33645365498 scopus 로고    scopus 로고
    • Coexpression of TorD enhances the transport of GFP via the TAT pathway
    • Li, S.Y., Chang, B.Y., and Lin, S.C. (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
  • 44
    • 0032479180 scopus 로고    scopus 로고
    • Expression of an antibody fragment at high levels in the bacterial cytoplasm
    • Martineau, P., Jones, P., and Winter, G. (1998) Expression of an antibody fragment at high levels in the bacterial cytoplasm. J Mol Biol 280: 117-127.
    • (1998) J Mol Biol , vol.280 , pp. 117-127
    • Martineau, P.1    Jones, P.2    Winter, G.3
  • 45
    • 84913705247 scopus 로고
    • The activation of mutant beta-galactosidase by specific antibodies
    • Miller, J.H, and Reznikoff, W.S, eds, Cold Spring Harbor, NY,USA: Cold Spring Harbor Laboratory Press, pp
    • Messer, W., and Melchers, F. (1978) The activation of mutant beta-galactosidase by specific antibodies. In The Operon. Miller, J.H., and Reznikoff, W.S. (eds). Cold Spring Harbor, NY,USA: Cold Spring Harbor Laboratory Press, pp. 305-315.
    • (1978) The Operon , pp. 305-315
    • Messer, W.1    Melchers, F.2
  • 46
    • 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., Fisher, A.C., Perlmutter, J.D., Hicks, M.G., Chanal, A., Santini, C.L., et al. (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
  • 47
    • 34547764371 scopus 로고    scopus 로고
    • Pimienta, E., Ayala, J.C., Rodriguez, C., Ramos, A., Van Mellaert, L., Vallin, C., and Anne, J. (2007) Recombinant production of Streptococcus equisimilis streptokinase by Streptomyces lividans. Microb Cell Fact 6: 20.
    • Pimienta, E., Ayala, J.C., Rodriguez, C., Ramos, A., Van Mellaert, L., Vallin, C., and Anne, J. (2007) Recombinant production of Streptococcus equisimilis streptokinase by Streptomyces lividans. Microb Cell Fact 6: 20.
  • 48
    • 0031841932 scopus 로고    scopus 로고
    • Effect of signal peptide changes on the extracellular processing of streptokinase from Escherichia coli: Requirement for secondary structure at the cleavage junction
    • Pratap, J., and Dikshit, K.L. (1998) Effect of signal peptide changes on the extracellular processing of streptokinase from Escherichia coli: requirement for secondary structure at the cleavage junction. Mol Gen Genet 258: 326-333.
    • (1998) Mol Gen Genet , vol.258 , pp. 326-333
    • Pratap, J.1    Dikshit, K.L.2
  • 49
    • 4444376602 scopus 로고    scopus 로고
    • mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N
    • Punginelli, C., Ize, B., Stanley, N.R., Stewart, V., Sawers, G., Berks, B.C., and Palmer, T. (2004) mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N. J Bacteriol 186: 6311-6315.
    • (2004) J Bacteriol , vol.186 , pp. 6311-6315
    • Punginelli, C.1    Ize, B.2    Stanley, N.R.3    Stewart, V.4    Sawers, G.5    Berks, B.C.6    Palmer, T.7
  • 50
    • 34248216120 scopus 로고    scopus 로고
    • A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding
    • Ribnicky, B., Van Blarcom, T., and Georgiou, G. (2007) A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding. J Mol Biol 369: 631-639.
    • (2007) J Mol Biol , vol.369 , pp. 631-639
    • Ribnicky, B.1    Van Blarcom, T.2    Georgiou, G.3
  • 51
    • 36348950408 scopus 로고    scopus 로고
    • Functional Tat transport of unstructured, small, hydrophilic proteins
    • Richter, S., Lindenstrauss, U., Lucke, C., Bayliss, R., and Bruser, T. (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
  • 52
    • 33646107403 scopus 로고    scopus 로고
    • Improved periplasmic production of biologically active murine interleukin-2 in Escherichia coli through a single aminoacid change at the cleavage site
    • Robbens, J., De Coen, W., Fiers, W., and Remaut, E. (2006) Improved periplasmic production of biologically active murine interleukin-2 in Escherichia coli through a single aminoacid change at the cleavage site. Proc Biochem 41: 1343-1346.
    • (2006) Proc Biochem , vol.41 , pp. 1343-1346
    • Robbens, J.1    De Coen, W.2    Fiers, W.3    Remaut, E.4
  • 53
    • 0035350689 scopus 로고    scopus 로고
    • Protein targeting by the twin-arginine translocation pathway
    • Robinson, C., and Bolhuis, A. (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
  • 54
    • 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., and Wu, L.F. (1999) Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial tat pathway. J Biol Chem 274: 13223-13228.
    • (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
  • 55
    • 4143083662 scopus 로고    scopus 로고
    • Comparison of the Sec and Tat secretion pathways for heterologous protein production by Streptomyces lividans
    • Schaerlaekens, K., Lammertyn, E., Geukens, N., De Keersmaeker, S., Anne, J., and Van Mellaert, L. (2004) Comparison of the Sec and Tat secretion pathways for heterologous protein production by Streptomyces lividans. J Biotechnol 112: 279-288.
    • (2004) J Biotechnol , vol.112 , pp. 279-288
    • Schaerlaekens, K.1    Lammertyn, E.2    Geukens, N.3    De Keersmaeker, S.4    Anne, J.5    Van Mellaert, L.6
  • 56
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and Dobberstein, B. (1996) Common principles of protein translocation across membranes. Science 271: 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 57
    • 0141727632 scopus 로고    scopus 로고
    • The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway
    • Schierle, C.F., Berkmen, M., Huber, D., Kumamoto, C., Boyd, D., and Beckwith, J. (2003) The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. J Bacteriol 185: 5706-5713.
    • (2003) J Bacteriol , vol.185 , pp. 5706-5713
    • Schierle, C.F.1    Berkmen, M.2    Huber, D.3    Kumamoto, C.4    Boyd, D.5    Beckwith, J.6
  • 58
    • 0030722626 scopus 로고    scopus 로고
    • Settles, A.M., Yonetani, A., Baron, A., Bush, D.R., Cline, K., and Martienssen, R. (1997) Sec-independent protein translocation by the maize Hcf106 protein. Science 278: 1467-1470.
    • Settles, A.M., Yonetani, A., Baron, A., Bush, D.R., Cline, K., and Martienssen, R. (1997) Sec-independent protein translocation by the maize Hcf106 protein. Science 278: 1467-1470.
  • 59
    • 0020320406 scopus 로고
    • Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane
    • Shuman, H.A. (1982) Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane. J Biol Chem 257: 5455-5461.
    • (1982) J Biol Chem , vol.257 , pp. 5455-5461
    • Shuman, H.A.1
  • 60
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith, G.P. (1985) Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228: 1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 61
    • 0030965606 scopus 로고    scopus 로고
    • Roles of disulfide bonds in bacterial alkaline phosphatase
    • Sone, M., Kishigami, S., Yoshihisa, T., and Ito, K. (1997) Roles of disulfide bonds in bacterial alkaline phosphatase. J Biol Chem 272: 6174-6178.
    • (1997) J Biol Chem , vol.272 , pp. 6174-6178
    • Sone, M.1    Kishigami, S.2    Yoshihisa, T.3    Ito, K.4
  • 62
    • 34247615394 scopus 로고    scopus 로고
    • A bacterial twohybrid system based on the twin-arginine transporter pathway of E. coli
    • Strauch, E.M., and Georgiou, G. (2007) A bacterial twohybrid system based on the twin-arginine transporter pathway of E. coli. Protein Sci 16: 1001-1008.
    • (2007) Protein Sci , vol.16 , pp. 1001-1008
    • Strauch, E.M.1    Georgiou, G.2
  • 63
    • 0035313153 scopus 로고    scopus 로고
    • Advances in Escherichia coli production of therapeutic proteins
    • Swartz, J.R. (2001) Advances in Escherichia coli production of therapeutic proteins. Curr Opin Biotechnol 12: 195-201.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 195-201
    • Swartz, J.R.1
  • 64
    • 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., Daniel, R.A., Errington, J., and 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
  • 66
    • 0347192985 scopus 로고    scopus 로고
    • Van den Berg, B., Clemons, W.M., Modis, Jr., Collinson, I., Hartmann, Y., Harrison, E., et al. (2004) X-ray structure of a protein-conducting channel. Nature 427: 36-44.
    • Van den Berg, B., Clemons, W.M., Modis, Jr., Collinson, I., Hartmann, Y., Harrison, E., et al. (2004) X-ray structure of a protein-conducting channel. Nature 427: 36-44.
  • 67
    • 0032478550 scopus 로고    scopus 로고
    • A novel and ubiquitous system for membrane targeting and secretion of cofactorcontaining proteins
    • Weiner, J.H., Bilous, P.T., Shaw, G.M., Lubitz, S.P., Frost, L., Thomas, G.H., et al. (1998) A novel and ubiquitous system for membrane targeting and secretion of cofactorcontaining 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
  • 68
    • 0035852714 scopus 로고    scopus 로고
    • The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization
    • Zhu, J., and Winans, S.C. (2001) The quorum-sensing transcriptional regulator TraR requires its cognate signaling ligand for protein folding, protease resistance, and dimerization. Proc Natl Acad Sci USA 98: 1507-1512.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1507-1512
    • Zhu, J.1    Winans, S.C.2
  • 69
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31: 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1


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