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Volumn 23, Issue 4, 2005, Pages 475-481

Extracellular secretion of polypeptides using a modified Escherichia coli flagellar secretion apparatus

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; ESCHERICHIA COLI; GENES; PROTEINS;

EID: 23644433830     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt1077     Document Type: Article
Times cited : (85)

References (34)
  • 1
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • Choi, J.H. & Lee, S.Y. Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl. Microbiol. Biotechnol. 64, 625-635 (2004).
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 2
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow secretion across the bacterial outer membrane
    • Thanassi, D.G. & Hultgren, S.J. Multiple pathways allow secretion across the bacterial outer membrane. Curr. Opin. Cell Biol. 12, 420-30 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 3
    • 0141941678 scopus 로고    scopus 로고
    • Establishing order for type III secretion substrates - A hierarchial process
    • Thomas, N.A. & Finley, B.B. Establishing order for type III secretion substrates - a hierarchial process. Trends Microbiol. 11, 398-403.
    • Trends Microbiol. , vol.11 , pp. 398-403
    • Thomas, N.A.1    Finley, B.B.2
  • 4
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins, C.E. & Galán, J. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414, 77-81 (2001).
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galán, J.2
  • 5
    • 0037453098 scopus 로고    scopus 로고
    • Type III secretion systems and bacterial flagella: Insights into their function from structural similarities
    • Blocker, A., Komoriya, K. & Aizawa, S.-I. Type III secretion systems and bacterial flagella: insights into their function from structural similarities. Pmc. Natl. Acad. Sci. USA 100, 3021-3030 (2003).
    • (2003) Pmc. Natl. Acad. Sci. USA , vol.100 , pp. 3021-3030
    • Blocker, A.1    Komoriya, K.2    Aizawa, S.-I.3
  • 6
    • 2642559479 scopus 로고    scopus 로고
    • Self-assembly and type III protein export of the bacterial flagellum
    • Minamino, T. & Namba, K. Self-assembly and type III protein export of the bacterial flagellum. J. Mol. Microbiol. Biotechnol. 7, 5-17 (2004).
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.7 , pp. 5-17
    • Minamino, T.1    Namba, K.2
  • 7
    • 0033003131 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: An mRNA signal that couples translation and secretion of YopQ
    • Anderson, D.M. & Schneewind, O. Yersinia enterocolitica type III secretion: an mRNA signal that couples translation and secretion of YopQ. Mol. Microbiol. 31, 1139-1148 (1999).
    • (1999) Mol. Microbiol. , vol.31 , pp. 1139-1148
    • Anderson, D.M.1    Schneewind, O.2
  • 8
    • 0035151519 scopus 로고    scopus 로고
    • Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals
    • Lloyd, S.A., Norman, M., Rosqvist, R. & Wolf-Watz, H. Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals. Mol. Microbiol. 39, 520-531 (2001).
    • (2001) Mol. Microbiol. , vol.39 , pp. 520-531
    • Lloyd, S.A.1    Norman, M.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 10
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • Parsot, C., Hamiaux, C. & Page, A.-L. The various and varying roles of specific chaperones in type III secretion systems. Curr. Opin. Microbiol. 6, 7-14 (2003).
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1    Hamiaux, C.2    Page, A.-L.3
  • 11
    • 0141618445 scopus 로고    scopus 로고
    • Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion
    • Evdokimov, A.G. et al. Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion. Nat. Struct. Biol 10, 789-793 (2003).
    • (2003) Nat. Struct. Biol , vol.10 , pp. 789-793
    • Evdokimov, A.G.1
  • 12
    • 0033033304 scopus 로고    scopus 로고
    • A new pathway for the secretion of virulence factors by bacteria: The flagellar export apparatus functions as a protein-secretion system
    • Young, G.M., Schmiel, D.H. & Miller, V.L. A new pathway for the secretion of virulence factors by bacteria: The flagellar export apparatus functions as a protein-secretion system. Proc. Natl. Acad. Sci. USA 96, 6456-6461 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6456-6461
    • Young, G.M.1    Schmiel, D.H.2    Miller, V.L.3
  • 13
    • 0942279512 scopus 로고    scopus 로고
    • Salmonella type III secretion-associated chaperones confer secretion-pathway specificity
    • Lee, S.H. & Galán, J.A. Salmonella type III secretion-associated chaperones confer secretion-pathway specificity. Mol. Microbiol. 51, 483-495 (2004).
    • (2004) Mol. Microbiol. , vol.51 , pp. 483-495
    • Lee, S.H.1    Galán, J.A.2
  • 14
    • 2442705402 scopus 로고    scopus 로고
    • Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus
    • Konkel, M.E. et al. Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus. J. Bacteriol. 186, 3296-3303 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 3296-3303
    • Konkel, M.E.1
  • 15
    • 0034444676 scopus 로고    scopus 로고
    • Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar Typhiurium and Escherichia coli
    • Chilcott, G.S. & Hughes, KT. Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar Typhiurium and Escherichia coli. Microbiol. Mol. Biol. Rev. 64, 694-708 (2000).
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 694-708
    • Chilcott, G.S.1    Hughes, K.T.2
  • 16
    • 0033817669 scopus 로고    scopus 로고
    • Completion of the hook-basal body complex of the Salmonella typhimurium flagellum is coupled to FIgM secretion and fliC transcription
    • Karlinsey, J.E. et al. Completion of the hook-basal body complex of the Salmonella typhimurium flagellum is coupled to FIgM secretion and fliC transcription. Mol. Microbiol. 37, 1220-1231 (2000).
    • (2000) Mol. Microbiol. , vol.37 , pp. 1220-1231
    • Karlinsey, J.E.1
  • 17
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura, K., Maki-Yonekura, S. & Namba, K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424, 643-650 (2003).
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 18
    • 0025740667 scopus 로고
    • Type 1 fimbriae mutants of Escherichia coli K12: Characterization of recognized afimbriate strains and construction of new fim deletion mutants
    • Blomfield, I.C., McClain, M.S. & Eisenstein, B.I. Type 1 fimbriae mutants of Escherichia coli K12: characterization of recognized afimbriate strains and construction of new fim deletion mutants. Mol. Microbiol. 5, 1439-1445 (1991).
    • (1991) Mol. Microbiol. , vol.5 , pp. 1439-1445
    • Blomfield, I.C.1    McClain, M.S.2    Eisenstein, B.I.3
  • 19
    • 0031424379 scopus 로고    scopus 로고
    • Functional expression of adhesive peptides as fusions to Escherichia coli flagellin
    • Westerlund-Wikström, B. et al. Functional expression of adhesive peptides as fusions to Escherichia coli flagellin. Prot. Engin. 10, 1319-1326 (1997).
    • (1997) Prot. Engin. , vol.10 , pp. 1319-1326
    • Westerlund-Wikström, B.1
  • 20
    • 0000535851 scopus 로고
    • Nucleotide sequence of the gene for fibronectin-binding protein from Staphylococcus aureus: Use of this peptide sequence in the synthesis of biologically active peptides
    • Signas, C. et al. Nucleotide sequence of the gene for fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides. Proc. Natl. Acad. Sci. USA 86, 699-703 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 699-703
    • Signas, C.1
  • 21
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K12
    • Blattner, RR. et al. The complete genome sequence of Escherichia coli K12. Science 277, 1453-1463 (1997).
    • (1997) Science , vol.277 , pp. 1453-1463
    • Blattner, R.R.1
  • 22
    • 2142787652 scopus 로고
    • Export of an N-terminal fragment of Escherichia coli flagellin by a flagellum-specific pathway
    • Kuwajima, G. et al. Export of an N-terminal fragment of Escherichia coli flagellin by a flagellum-specific pathway. Proc. Natl. Acad. Sci. USA 86, 4953-4957 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4953-4957
    • Kuwajima, G.1
  • 23
    • 0033149857 scopus 로고    scopus 로고
    • Reevaluation of the promoter structure of the class 3 flagellar operons of Escherichia coli and Salmonella
    • Ide, N., Ikebe, T. & Kutsukake, K. Reevaluation of the promoter structure of the class 3 flagellar operons of Escherichia coli and Salmonella. Genes Genet. Syst. 74, 113-116 (1999).
    • (1999) Genes Genet. Syst. , vol.74 , pp. 113-116
    • Ide, N.1    Ikebe, T.2    Kutsukake, K.3
  • 24
    • 0027293062 scopus 로고
    • PEB1, the major cell-binding factor of Campylobacter jejuni, is a homolog of the binding component in Gram-negative nutrient transport systems
    • Pei, Z. & Blaser, MJ. PEB1, the major cell-binding factor of Campylobacter jejuni, is a homolog of the binding component in Gram-negative nutrient transport systems. J. Biol. Chem. 268, 18717-18725 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 18717-18725
    • Pei, Z.1    Blaser, M.J.2
  • 25
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed α-enolase of Streptococcus pneumoniae
    • Bergmann, S. et al. Identification of a novel plasmin(ogen)-binding motif in surface displayed α-enolase of Streptococcus pneumoniae. Mol. Microbiol. 49, 411-423 (2003).
    • (2003) Mol. Microbiol. , vol.49 , pp. 411-423
    • Bergmann, S.1
  • 26
    • 0032030760 scopus 로고    scopus 로고
    • Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants
    • Davis, S. & Vierstra, R.D. Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants. Plant Mol. Biol. 36, 521-528 (1998).
    • (1998) Plant Mol. Biol. , vol.36 , pp. 521-528
    • Davis, S.1    Vierstra, R.D.2
  • 27
    • 0023714467 scopus 로고
    • A short polypeptide marker sequence useful for recombinant protein identification and purification
    • Hopp, T.V. et al. A short polypeptide marker sequence useful for recombinant protein identification and purification. BioTechnology 6, 1204-1210 (1988).
    • (1988) BioTechnology , vol.6 , pp. 1204-1210
    • Hopp, T.V.1
  • 28
    • 2542582286 scopus 로고    scopus 로고
    • Periplasmic lysozyme inhibitor contributes to lysozyme resistance in Escherichia coli
    • Deckers, D. et al. Periplasmic lysozyme inhibitor contributes to lysozyme resistance in Escherichia coli. Cell. Mol. Life Sci. 61, 1229-1237 (2004).
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1229-1237
    • Deckers, D.1
  • 29
    • 0024467106 scopus 로고
    • Outer membrane barrier as a mechanism of antimicrobial resistance
    • Nikaido, H. Outer membrane barrier as a mechanism of antimicrobial resistance. Antimicrob. Agents Chemother. 33, 1831-1836 (1989).
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1831-1836
    • Nikaido, H.1
  • 30
    • 0037387967 scopus 로고    scopus 로고
    • Substrate specificity classes and the recognition for Salmonella type III flagellar export
    • Hirano, T., Minamino, T., Namba, K. & Macnab, R.M. Substrate specificity classes and the recognition for Salmonella type III flagellar export. J. Bacteriol. 185, 2485-2492 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 2485-2492
    • Hirano, T.1    Minamino, T.2    Namba, K.3    Macnab, R.M.4
  • 31
    • 0004136246 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA
    • rd edn. (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA, 2001).
    • (2001) rd Edn.
    • Sambrook, J.1    Russell, D.2
  • 32
    • 0026411101 scopus 로고
    • Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector
    • Donnenberg, M. & Kaper, J.B. Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector. Infect. Immun. 59, 4310-4317(1991).
    • (1991) Infect. Immun. , vol.59 , pp. 4310-4317
    • Donnenberg, M.1    Kaper, J.B.2
  • 33
    • 0027494612 scopus 로고
    • Isogenic P-fimbrial deletion mutants of pyelonephritogenic Escherichia coli: The role of αGal(1-4)βGal binding virulence of a wild-type strain
    • Mobley, H.L.T. et al. Isogenic P-fimbrial deletion mutants of pyelonephritogenic Escherichia coli: the role of αGal(1-4)βGal binding virulence of a wild-type strain. Mol. Microbiol. 10, 143-155 (1993).
    • (1993) Mol. Microbiol. , vol.10 , pp. 143-155
    • Mobley, H.L.T.1
  • 34
    • 0028180278 scopus 로고
    • PBBR1MCS: A broad-host-range cloning vector
    • Kovach, M.E. et al. pBBR1MCS: a broad-host-range cloning vector. Biotechniques. 16, 800-802 (1994).
    • (1994) Biotechniques , vol.16 , pp. 800-802
    • Kovach, M.E.1


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