메뉴 건너뛰기




Volumn 28, Issue 1, 2003, Pages 173-181

Expression of proteins using the third domain of the Escherichia coli periplasmic-protein TolA as a fusion partner

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; GOSSWEILERODENDRON BALSAMIFERUM;

EID: 0037360296     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00681-2     Document Type: Article
Times cited : (29)

References (28)
  • 1
    • 0028825817 scopus 로고
    • Gene fusion expression systems in Escherichia coli
    • E.R. LaVallie, J.M. McCoy, Gene fusion expression systems in Escherichia coli, Curr. Opin. Biotechnol. 6 (1995) 501-506.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 501-506
    • LaVallie, E.R.1    McCoy, J.M.2
  • 2
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • S.C. Makrides, Strategies for achieving high-level expression of genes in Escherichia coli, Microbiol. Rev. 60 (1996) 512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 3
    • 0028248993 scopus 로고
    • 6xHis-Ni-NTA chromatography as a superior technique in recombinant protein expression/purification
    • J. Crowe, H. Dobeli, R. Gentz, E. Hochuli, D. Stuber, K. Henco, 6xHis-Ni-NTA chromatography as a superior technique in recombinant protein expression/purification, Methods Mol. Biol. 31 (1994) 371-387.
    • (1994) Methods Mol. Biol. , vol.31 , pp. 371-387
    • Crowe, J.1    Dobeli, H.2    Gentz, R.3    Hochuli, E.4    Stuber, D.5    Henco, K.6
  • 4
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • D.B. Smith, K.S. Johnson, Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase, Gene 67 (1988) 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 6
    • 0026011001 scopus 로고
    • Enzyme immobilization using a cellulose-binding domain: Properties of a β-glucosidase fusion protein
    • E. Ong, N.R. Gilkes, R.C. Miller Jr., A.J. Warren, D.G. Kilburn, Enzyme immobilization using a cellulose-binding domain: properties of a β-glucosidase fusion protein, Enzyme Microb. Technol. 13 (1991) 59-65.
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 59-65
    • Ong, E.1    Gilkes, N.R.2    Miller R.C., Jr.3    Warren, A.J.4    Kilburn, D.G.5
  • 7
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • E.R. LaVallie, E.A. DiBlasio, S. Kovacic, K.L. Grant, P.F. Schendel, J.M. McCoy, A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm, Biotechnology (N. Y.) 11 (1993) 187-193.
    • (1993) Biotechnology (N. Y.) , vol.11 , pp. 187-193
    • LaVallie, E.R.1    DiBlasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 8
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • A.I. Derman, W.A. Prinz, D. Belin, J. Beckwith, Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli, Science 262 (1993) 1744-1747.
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 9
    • 0032189925 scopus 로고    scopus 로고
    • Disulfide bond formation in the Escherichia coli cytoplasm: An in vivo role reversal for the thioredoxins
    • E.J. Stewart, F. Aslund, J. Beckwith, Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins, EMBO J. 17 (1998) 5543-5550.
    • (1998) EMBO J. , vol.17 , pp. 5543-5550
    • Stewart, E.J.1    Aslund, F.2    Beckwith, J.3
  • 10
    • 0029115204 scopus 로고
    • Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA
    • L.A. Collins-Racie, J.M. McColgan, K.L. Grant, E.A. Diblasio-Smith, J.M. McCoy, E.R. LaVallie, Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA, Biotechnology (N. Y.) 13 (1995) 982-987.
    • (1995) Biotechnology (N. Y.) , vol.13 , pp. 982-987
    • Collins-Racie, L.A.1    McColgan, J.M.2    Grant, K.L.3    Diblasio-Smith, E.A.4    McCoy, J.M.5    LaVallie, E.R.6
  • 11
    • 0025912823 scopus 로고
    • TolA: A membrane protein involved in colicin uptake contains an extended helical region
    • S.K. Levengood, W.J. Beyer, R.E. Webster, TolA: a membrane protein involved in colicin uptake contains an extended helical region, Proc. Natl. Acad. Sci. USA 88 (1991) 5939-5943.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5939-5943
    • Levengood, S.K.1    Beyer, W.J.2    Webster, R.E.3
  • 13
    • 0032774018 scopus 로고    scopus 로고
    • The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability
    • J.C. Lazzaroni, P. Germon, M.C. Ray, A. Vianney, The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability, FEMS Microbiol. Lett. 177 (1999) 191-197:
    • (1999) FEMS Microbiol. Lett. , vol.177 , pp. 191-197
    • Lazzaroni, J.C.1    Germon, P.2    Ray, M.C.3    Vianney, A.4
  • 14
    • 0000046526 scopus 로고    scopus 로고
    • Filamentous phage infection: Crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA
    • J. Lubkowski, F. Hennecke, A. Pluckthun, A. Wlodawer, Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA, Structure Fold. Des. 7 (1999) 711-722.
    • (1999) Structure Fold. Des. , vol.7 , pp. 711-722
    • Lubkowski, J.1    Hennecke, F.2    Pluckthun, A.3    Wlodawer, A.4
  • 15
    • 0031799096 scopus 로고    scopus 로고
    • Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: A biophysical approach
    • E.M. Raggett, G. Bainbridge, L.J. Evans, A. Cooper, J.H. Lakey, Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: a biophysical approach, Mol. Microbiol. 28 (1998) 1335-1343.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1335-1343
    • Raggett, E.M.1    Bainbridge, G.2    Evans, L.J.3    Cooper, A.4    Lakey, J.H.5
  • 16
    • 0028347588 scopus 로고
    • Immunoglobulin-type domains of titin: Same fold, different stability?
    • A.S. Politou, M. Gautel, M. Pfuhl, S. Labeit, A. Pastore, Immunoglobulin-type domains of titin: same fold, different stability?, Biochemistry 33 (1994) 4730-4737.
    • (1994) Biochemistry , vol.33 , pp. 4730-4737
    • Politou, A.S.1    Gautel, M.2    Pfuhl, M.3    Labeit, S.4    Pastore, A.5
  • 17
    • 0036409194 scopus 로고    scopus 로고
    • Expression and one-step purification of a developmentally regulated protein from Dictyostelium discoideum
    • M. Ubeidat, C.L. Rutherford, Expression and one-step purification of a developmentally regulated protein from Dictyostelium discoideum, Protein Expression Purif. 25 (2002) 472-480.
    • (2002) Protein Expression Purif. , vol.25 , pp. 472-480
    • Ubeidat, M.1    Rutherford, C.L.2
  • 18
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • F. Baneyx, Recombinant protein expression in Escherichia coli, Curr. Opin. Biotechnol. 10 (1999) 411-421.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 20
    • 0036093944 scopus 로고    scopus 로고
    • The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB
    • A. Walburger, C. Lazdunski, Y. Corda, The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB, Mol. Microbiol. 44 (2002) 695-708.
    • (2002) Mol. Microbiol. , vol.44 , pp. 695-708
    • Walburger, A.1    Lazdunski, C.2    Corda, Y.3
  • 21
    • 0032190602 scopus 로고    scopus 로고
    • TolAIII co-overexpression facilitates the recovery of periplasmic recombinant Proteins into the growth medium of Escherichia coli
    • E.W.M. Wan, F. Baneyx, TolAIII co-overexpression facilitates the recovery of periplasmic recombinant Proteins into the growth medium of Escherichia coli, Protein Expression Purif. 14 (1998) 13-22.
    • (1998) Protein Expression Purif. , vol.14 , pp. 13-22
    • Wan, E.W.M.1    Baneyx, F.2
  • 22
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • J.F. Kane, Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli, Curr. Opin. Biotechnol. 6 (1995) 494-500.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 23
    • 0025166089 scopus 로고
    • Secondary structure of the ribosome binding site determines translational efficiency: A quantitative analysis
    • M.H. de Smit, J. van Duin, Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis, Proc. Natl. Acad. Sci. USA 87 (1990) 7668-7672.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7668-7672
    • De Smit, M.H.1    Van Duin, J.2
  • 24
    • 0242722703 scopus 로고    scopus 로고
    • Prokaryotic in vivo expression systems
    • S.J. Higgins, et al. (Eds.), Oxford University Press, Oxford
    • E.R. Appelbaum, A.R. Shatzman, Prokaryotic in vivo expression systems, in: S.J. Higgins, et al. (Eds.), Protein Expression, a Practical Approach, Oxford University Press, Oxford, 2002, pp. 169-200.
    • (2002) Protein Expression, a Practical Approach , pp. 169-200
    • Appelbaum, E.R.1    Shatzman, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.