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Volumn 14, Issue 1, 2004, Pages 128-133

Secretion capacity limitations of the Sec pathway in Escherichia coli

Author keywords

Proinsulin; Secretion; Secretory protein

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; HYBRID PROTEIN; PROINSULIN; STAPHYLOCOCCUS PROTEIN A;

EID: 1542285366     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (21)

References (62)
  • 1
    • 0025938675 scopus 로고
    • A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coli
    • Andersson, H. and G. von Heijne. 1991. A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 88: 9751-9754.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9751-9754
    • Andersson, H.1    von Heijne, G.2
  • 2
    • 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
  • 3
    • 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., L. F. Wu, J. Brunner, and M. Muller. 2000. Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor. EMBO J. 19: 134-143.
    • (2000) EMBO J. , vol.19 , pp. 134-143
    • Beck, K.1    Wu, L.F.2    Brunner, J.3    Muller, M.4
  • 4
    • 0032577555 scopus 로고    scopus 로고
    • Requirements for the translocation of elongation-arrested, ribosome-associated OmpA across the plasma membrane of Escherichia coli
    • Behrmann, M., H. G. Koch, T. Hengelage, B. Wieseler, H. K. Hoffschulte, and M. Muller. 1998. Requirements for the translocation of elongation-arrested, ribosome-associated OmpA across the plasma membrane of Escherichia coli. J. Biol. Chem. 273: 13898-13904.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13898-13904
    • Behrmann, M.1    Koch, H.G.2    Hengelage, T.3    Wieseler, B.4    Hoffschulte, H.K.5    Muller, M.6
  • 6
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • Breyton, C., W. Haase, T. A. Rapoport, W. Kuhlbrandt, and I. Collinson. 2002. Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature 418: 662-665.
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kuhlbrandt, W.4    Collinson, I.5
  • 7
    • 0035029582 scopus 로고    scopus 로고
    • Biogenesis of inner membrane proteins in Escherichia coli
    • de Gier, J. W. and J. Luirink. 2001. Biogenesis of inner membrane proteins in Escherichia coli. Mol. Microbiol. 40: 314-322.
    • (2001) Mol. Microbiol. , vol.40 , pp. 314-322
    • de Gier, J.W.1    Luirink, J.2
  • 8
    • 0028907619 scopus 로고
    • Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction
    • Dong, H., L. Nilsson, and C. G. Kurland. 1995. Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction. J. Bacteriol. 177: 1497-1504.
    • (1995) J. Bacteriol. , vol.177 , pp. 1497-1504
    • Dong, H.1    Nilsson, L.2    Kurland, C.G.3
  • 9
    • 0032809760 scopus 로고    scopus 로고
    • Following the leader: Bacterial protein export through the See pathway
    • Economou, A. 1999. Following the leader: bacterial protein export through the See pathway. Trends Microbiol. 7: 315-320.
    • (1999) Trends Microbiol. , vol.7 , pp. 315-320
    • Economou, A.1
  • 10
    • 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
  • 11
    • 0033008601 scopus 로고    scopus 로고
    • Protein targeting to the bacterial cytoplasmic membrane
    • Fekkes, P. and A. J. Driessen. 1999. Protein targeting to the bacterial cytoplasmic membrane. Microbiol. Mol. Biol. Rev. 63: 161-173.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 161-173
    • Fekkes, P.1    Driessen, A.J.2
  • 13
    • 85041115207 scopus 로고    scopus 로고
    • New prospects in studying the bacterial signal recognition particle pathway
    • Herskovits, A. A., E. S. Bochkareva, and E. Bibi. 2000. New prospects in studying the bacterial signal recognition particle pathway. Mol. Microbiol. 38: 927-939.
    • (2000) Mol. Microbiol. , vol.38 , pp. 927-939
    • Herskovits, A.A.1    Bochkareva, E.S.2    Bibi, E.3
  • 14
    • 0030881913 scopus 로고    scopus 로고
    • The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
    • Hesterkamp, T., E. Deuerling, and B. Bukau. 1997. The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J. Biol. Chem. 272: 21865-21871.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21865-21871
    • Hesterkamp, T.1    Deuerling, E.2    Bukau, B.3
  • 15
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains
    • Hesterkamp, T., S. Hauser, H. Lutcke, and B. Bukau. 1996. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc. Natl. Acad. Sci. USA 93: 4437-4441.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4437-4441
    • Hesterkamp, T.1    Hauser, S.2    Lutcke, H.3    Bukau, B.4
  • 16
    • 0023449557 scopus 로고
    • Conformation of protein secreted across bacterial outer membranes: A study of enterotoxin translocation from Vibrio cholerae
    • Hirst, T. R. and J. Holmgren. 1987. Conformation of protein secreted across bacterial outer membranes: A study of enterotoxin translocation from Vibrio cholerae. Proc. Natl. Acad. Sci. USA 84: 7418-7422.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7418-7422
    • Hirst, T.R.1    Holmgren, J.2
  • 17
    • 0035830914 scopus 로고    scopus 로고
    • The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli
    • Huang, H. C., M. Y. Sherman, O. Kandror, and A. L. Goldberg. 2001. The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli. J. Biol. Chem. 276: 3920-3928.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3920-3928
    • Huang, H.C.1    Sherman, M.Y.2    Kandror, O.3    Goldberg, A.L.4
  • 18
    • 0032924410 scopus 로고    scopus 로고
    • Metabolic alarms and cell division in Escherichia coli
    • Joseleau-Petit, D., D. Vinella, and R. D'Ari. 1999. Metabolic alarms and cell division in Escherichia coli. J. Bacteriol. 181: 9-14.
    • (1999) J. Bacteriol. , vol.181 , pp. 9-14
    • Joseleau-Petit, D.1    Vinella, D.2    D'Ari, R.3
  • 19
    • 0034029906 scopus 로고    scopus 로고
    • The net charge of the first 18 residues of the mature sequence affects protein translocation across the cytoplasmic membrane of gram-negative bacteria
    • Kajava, A. V., S. N. Zolov, A. E. Kalinin, and M. A. Nesmeyanova. 2000. The net charge of the first 18 residues of the mature sequence affects protein translocation across the cytoplasmic membrane of gram-negative bacteria. J. Bacteriol. 182: 2163-2169.
    • (2000) J. Bacteriol. , vol.182 , pp. 2163-2169
    • Kajava, A.V.1    Zolov, S.N.2    Kalinin, A.E.3    Nesmeyanova, M.A.4
  • 20
    • 0033945367 scopus 로고    scopus 로고
    • SecB dependence of an exported protein is a continuum influenced by the characteristics of the signal peptide or early mature region
    • Kim, J., J. Luirink, and D. A. Kendall. 2000. SecB dependence of an exported protein is a continuum influenced by the characteristics of the signal peptide or early mature region. J. Bacteriol. 182: 4108-4112.
    • (2000) J. Bacteriol. , vol.182 , pp. 4108-4112
    • Kim, J.1    Luirink, J.2    Kendall, D.A.3
  • 21
    • 0033735427 scopus 로고    scopus 로고
    • Protein secretion mechanisms in Gram-negative bacteria
    • Koster, M., W. Bitter, and J. Tommassen. 2000. Protein secretion mechanisms in Gram-negative bacteria. Int. J. Med. Microbiol. 290: 325-331.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 325-331
    • Koster, M.1    Bitter, W.2    Tommassen, J.3
  • 22
    • 0035916409 scopus 로고    scopus 로고
    • Secretory production of Arthrobacter levan fructotransferase from recombinant Escherichia coli
    • Lee, J., V. Saraswat, I. Koh, K. B. Song, Y. H. Park, and S. K. Rhee. 2001. Secretory production of Arthrobacter levan fructotransferase from recombinant Escherichia coli. FEMS Microbiol. Lett. 195: 127-132.
    • (2001) FEMS Microbiol. Lett. , vol.195 , pp. 127-132
    • Lee, J.1    Saraswat, V.2    Koh, I.3    Song, K.B.4    Park, Y.H.5    Rhee, S.K.6
  • 23
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides, S. C. 1996. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60: 512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 24
    • 0033943049 scopus 로고    scopus 로고
    • Escherichia coli translocase: The unravelling of a molecular machine
    • Manting, E. H. and A. J. Driessen. 2000. Escherichia coli translocase: the unravelling of a molecular machine. Mol. Microbiol. 37: 226-238.
    • (2000) Mol. Microbiol. , vol.37 , pp. 226-238
    • Manting, E.H.1    Driessen, A.J.2
  • 25
    • 0034254190 scopus 로고    scopus 로고
    • Elongation arrest is a physiologically important function of signal recognition particle
    • Mason, N., L. F. Ciufo, and J. D. Brown. 2000. Elongation arrest is a physiologically important function of signal recognition particle. EMBO J. 19: 4164-4174.
    • (2000) EMBO J. , vol.19 , pp. 4164-4174
    • Mason, N.1    Ciufo, L.F.2    Brown, J.D.3
  • 26
    • 0033757725 scopus 로고    scopus 로고
    • Recombinant human proinsulin: A new approach in gene assembly and protein expression
    • Mergulhão, F., G. Monteiro, A. Kelly, M. Taipa, and J. Cabral. 2000. Recombinant human proinsulin: A new approach in gene assembly and protein expression. J. Microbiol. Biotechnol. 10: 690-693.
    • (2000) J. Microbiol. Biotechnol. , vol.10 , pp. 690-693
    • Mergulhão, F.1    Monteiro, G.2    Kelly, A.3    Taipa, M.4    Cabral, J.5
  • 27
    • 0037899027 scopus 로고    scopus 로고
    • Medium and copy number effects on the secretion of human proinsulin in Escherichia coli using the universal stress promoters uspA and uspB
    • Mergulhão, F., G. Monteiro, G. Larsson, A. Sandem, A. Farewell, T. Nystrom, J. Cabral, and M. Taipa. 2003. Medium and copy number effects on the secretion of human proinsulin in Escherichia coli using the universal stress promoters uspA and uspB. Appl. Microbiol. Biotechnol. 61: 495-501.
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 495-501
    • Mergulhão, F.1    Monteiro, G.2    Larsson, G.3    Sandem, A.4    Farewell, A.5    Nystrom, T.6    Cabral, J.7    Taipa, M.8
  • 29
    • 0035168991 scopus 로고    scopus 로고
    • A quantitative ELISA for monitoring the secretion of ZZ-fusion proteins using SpA domain as immunodetection reporter system
    • Mergulhão, F. J., G. A. Monteiro, J. M. Cabral, and M. A. Taipa. 2001. A quantitative ELISA for monitoring the secretion of ZZ-fusion proteins using SpA domain as immunodetection reporter system. Mol. Biotechnol. 19: 239-244.
    • (2001) Mol. Biotechnol. , vol.19 , pp. 239-244
    • Mergulhão, F.J.1    Monteiro, G.A.2    Cabral, J.M.3    Taipa, M.A.4
  • 31
    • 0031985197 scopus 로고    scopus 로고
    • Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon
    • Miller, K. W., R. Schamber, Y. Chen, and B. Ray. 1998. Production of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon. Appl. Environ. Microbiol. 64: 14-20.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 14-20
    • Miller, K.W.1    Schamber, R.2    Chen, Y.3    Ray, B.4
  • 32
    • 0031081341 scopus 로고    scopus 로고
    • Protein misfolding in the cell envelope of Escherichia coli: New signaling pathways
    • Missiakas, D. and S. Raina. 1997. Protein misfolding in the cell envelope of Escherichia coli: New signaling pathways. Trends Biochem. Sci. 22: 59-63.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 59-63
    • Missiakas, D.1    Raina, S.2
  • 33
    • 0025933503 scopus 로고
    • Expert system for predicting protein localization sites in gram-negative bacteria
    • Nakai, K. and M. Kanehisa. 1991. Expert system for predicting protein localization sites in gram-negative bacteria. Proteins 11: 95-110.
    • (1991) Proteins , vol.11 , pp. 95-110
    • Nakai, K.1    Kanehisa, M.2
  • 34
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10: 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 35
    • 0033557759 scopus 로고    scopus 로고
    • Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation
    • Nishiyama, K., A. Fukuda, K. Morita, and H. Tokuda. 1999. Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation. EMBO J. 18: 1049-1058.
    • (1999) EMBO J. , vol.18 , pp. 1049-1058
    • Nishiyama, K.1    Fukuda, A.2    Morita, K.3    Tokuda, H.4
  • 36
    • 0036015653 scopus 로고    scopus 로고
    • SecDFyajC forms a heterotetrameric complex with YidC
    • Nouwen, N. and A. J. Driessen. 2002. SecDFyajC forms a heterotetrameric complex with YidC. Mol. Microbiol. 44: 1397-1405.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1397-1405
    • Nouwen, N.1    Driessen, A.J.2
  • 37
    • 0031709169 scopus 로고    scopus 로고
    • Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon
    • Oliver, D., J. Norman, and S. Sarker. 1998. Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon. J. Bacteriol. 180: 5240-5242.
    • (1998) J. Bacteriol. , vol.180 , pp. 5240-5242
    • Oliver, D.1    Norman, J.2    Sarker, S.3
  • 38
    • 0030064497 scopus 로고    scopus 로고
    • Effect of signal peptide alterations and replacement on export of xylanase A in Streptomyces lividans
    • Page, N., D. Kluepfel, F. Shareck, and R. Morosoli. 1996. Effect of signal peptide alterations and replacement on export of xylanase A in Streptomyces lividans. Appl. Environ. Microbiol. 62: 109-114.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 109-114
    • Page, N.1    Kluepfel, D.2    Shareck, F.3    Morosoli, R.4
  • 39
    • 0035142648 scopus 로고    scopus 로고
    • Subset of hybrid eukaryotic proteins is exported by the type I secretion system of Erwinia chrysanthemi
    • Palacios, J. L., I. Zaror, P. Martinez, F. Uribe, P. Opazo, T. Socias, M. Gidekel, and A. Venegas. 2001. Subset of hybrid eukaryotic proteins is exported by the type I secretion system of Erwinia chrysanthemi. J. Bacteriol. 183: 1346-1358.
    • (2001) J. Bacteriol. , vol.183 , pp. 1346-1358
    • Palacios, J.L.1    Zaror, I.2    Martinez, P.3    Uribe, F.4    Opazo, P.5    Socias, T.6    Gidekel, M.7    Venegas, A.8
  • 41
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz, W. A., F. Aslund, A. Holmgren, and J. Beckwith. 1997. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272: 15661-15667.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 42
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57: 50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 43
    • 0031940586 scopus 로고    scopus 로고
    • Isolation of recombinant secretory proteins by limited induction and quantitative harvest
    • Rosenberg, H. F. 1998. Isolation of recombinant secretory proteins by limited induction and quantitative harvest. Biotechniques 24: 188-191.
    • (1998) Biotechniques , vol.24 , pp. 188-191
    • Rosenberg, H.F.1
  • 46
    • 0036223671 scopus 로고    scopus 로고
    • Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulation
    • Sarker, S. and D. Oliver. 2002. Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulation. J. Bacteriol. 184: 2360-2369.
    • (2002) J. Bacteriol. , vol.184 , pp. 2360-2369
    • Sarker, S.1    Oliver, D.2
  • 47
    • 0033801865 scopus 로고    scopus 로고
    • Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression
    • Sarker, S., K. E. Rudd, and D. Oliver. 2000. Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression. J. Bacteriol. 182: 5592-5595.
    • (2000) J. Bacteriol. , vol.182 , pp. 5592-5595
    • Sarker, S.1    Rudd, K.E.2    Oliver, D.3
  • 48
    • 0029128930 scopus 로고
    • Extracellular secretion of pullulanase is unaffected by minor sequence changes but is usually prevented by adding reporter proteins to its N- or C-terminal end
    • Sauvonnet, N., I. Poquet, and A. P. Pugsley. 1995. Extracellular secretion of pullulanase is unaffected by minor sequence changes but is usually prevented by adding reporter proteins to its N- or C-terminal end. J. Bacteriol. 177: 5238-5246.
    • (1995) J. Bacteriol. , vol.177 , pp. 5238-5246
    • Sauvonnet, N.1    Poquet, I.2    Pugsley, A.P.3
  • 49
    • 0033230145 scopus 로고    scopus 로고
    • Secretion-dependent proteolysis of heterologous protein by recombinant Escherichia coli is connected to an increased activity of the energy-generating dissimilatory pathway
    • Schmidt, M., E. Viaplana, F. Hoffmann, S. Marten, A. Villaverde, and U. Rinas. 1999. Secretion-dependent proteolysis of heterologous protein by recombinant Escherichia coli is connected to an increased activity of the energy-generating dissimilatory pathway. Biotechnol. Bioeng. 66: 61-67.
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 61-67
    • Schmidt, M.1    Viaplana, E.2    Hoffmann, F.3    Marten, S.4    Villaverde, A.5    Rinas, U.6
  • 50
    • 9244231763 scopus 로고    scopus 로고
    • Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli
    • Simmons, L. C. and D. G. Yansura. 1996. Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli. Nat. Biotechnol. 14: 629-634.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 629-634
    • Simmons, L.C.1    Yansura, D.G.2
  • 52
    • 0024316915 scopus 로고
    • A conservative amino acid substitution, arginine for lysine, abolishes export of a hybrid protein in Escherichia coli. Implications for the mechanism of protein secretion
    • Summers, R. G., C. R. Harris, and J. R. Knowles. 1989. A conservative amino acid substitution, arginine for lysine, abolishes export of a hybrid protein in Escherichia coli. Implications for the mechanism of protein secretion. J. Biol. Chem. 264: 20082-20088.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20082-20088
    • Summers, R.G.1    Harris, C.R.2    Knowles, J.R.3
  • 53
    • 0024388902 scopus 로고
    • Illicit secretion of a cytoplasmic protein into the periplasm of Escherichia coli requires a signal peptide plus a portion of the cognate secreted protein. Demarcation of the critical region of the mature protein
    • Summers, R. G. and J. R. Knowles. 1989. Illicit secretion of a cytoplasmic protein into the periplasm of Escherichia coli requires a signal peptide plus a portion of the cognate secreted protein. Demarcation of the critical region of the mature protein. J. Biol. Chem. 264: 20074-20081.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20074-20081
    • Summers, R.G.1    Knowles, J.R.2
  • 54
    • 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
  • 55
    • 0036093705 scopus 로고    scopus 로고
    • Engineering a novel secretion signal for cross-host recombinant protein expression
    • Tan, N. S., B. Ho, and J. L. Ding. 2002. Engineering a novel secretion signal for cross-host recombinant protein expression. Protein Eng. 15: 337-345.
    • (2002) Protein Eng. , vol.15 , pp. 337-345
    • Tan, N.S.1    Ho, B.2    Ding, J.L.3
  • 56
    • 0036135526 scopus 로고    scopus 로고
    • Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway
    • Tian, H. and J. Beckwith. 2002. Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway. J. Bacteriol. 184: 111-118.
    • (2002) J. Bacteriol. , vol.184 , pp. 111-118
    • Tian, H.1    Beckwith, J.2
  • 57
    • 0035374515 scopus 로고    scopus 로고
    • Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity
    • Triplett, T. L., A. R. Sgrignoli, F. B. Gao, Y. B. Yang, P. C. Tai, and L. M. Gierasch. 2001. Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity. J. Biol. Chem. 276: 19648-19655.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19648-19655
    • Triplett, T.L.1    Sgrignoli, A.R.2    Gao, F.B.3    Yang, Y.B.4    Tai, P.C.5    Gierasch, L.M.6
  • 59
    • 0032125782 scopus 로고    scopus 로고
    • PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation
    • van der Wolk, J. P., P. Fekkes, A. Boorsma, J. L. Huie, T. J. Silhavy, and A. J. Driessen. 1998. PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation. EMBO J. 17: 3631-3639.
    • (1998) EMBO J. , vol.17 , pp. 3631-3639
    • van der Wolk, J.P.1    Fekkes, P.2    Boorsma, A.3    Huie, J.L.4    Silhavy, T.J.5    Driessen, A.J.6
  • 60
    • 0035980042 scopus 로고    scopus 로고
    • Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis
    • Veenendaal, A. K., C. van der Does, and A. J. Driessen. 2001. Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis. J. Biol Chem. 276: 32559-32566.
    • (2001) J. Biol Chem. , vol.276 , pp. 32559-32566
    • Veenendaal, A.K.1    van der Does, C.2    Driessen, A.J.3
  • 61
    • 0034616343 scopus 로고    scopus 로고
    • Signal peptide determinants of SecA binding and stimulation of ATPase activity
    • Wang, L., A. Miller, and D. A. Kendall. 2000. Signal peptide determinants of SecA binding and stimulation of ATPase activity. J. Biol. Chem. 275: 10154-10159.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10154-10159
    • Wang, L.1    Miller, A.2    Kendall, D.A.3
  • 62
    • 0034663803 scopus 로고    scopus 로고
    • Evaluating the oligomeric state of SecYEG in preprotein translocase
    • Yahr, T. L. and W. T. Wickner. 2000. Evaluating the oligomeric state of SecYEG in preprotein translocase. EMBO J. 19: 4393-4401.
    • (2000) EMBO J. , vol.19 , pp. 4393-4401
    • Yahr, T.L.1    Wickner, W.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.