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Volumn 287, Issue 12, 2012, Pages 9259-9268

Two distinct states of Escherichia coli cells that overexpress recombinant heterogeneous β-galactosidase

Author keywords

[No Author keywords available]

Indexed keywords

ASPERGILLUS PHOENICIS; CELL POPULATIONS; CELL STATE; DYNAMIC PROCESS; E. COLI; ESCHERICHIA COLI CELLS; EXPRESSION LEVELS; GALACTOSIDASES; IN-VIVO; INCLUSION BODIES; INDIVIDUAL CELLS; LEVEL CHANGE; PROTEIN EXPRESSIONS; RED FLUORESCENCE; TWO-STATE; WESTERN BLOTTING;

EID: 84863351064     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.327668     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 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
  • 2
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • Schein, C. H. (1989) Production of soluble recombinant proteins in bacteria. Nat. Biotechnol. 7, 1141-1149
    • (1989) Nat. Biotechnol. , vol.7 , pp. 1141-1149
    • Schein, C.H.1
  • 3
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sørensen, H. P., and Mortensen, K. K. (2005) Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb. Cell Fact. 4, 1
    • (2005) Microb. Cell Fact. , vol.4 , pp. 1
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 4
    • 0025570018 scopus 로고
    • Chaperonin assisted polypeptide folding and assembly. Implications for the production of functional proteins in bacteria
    • Gatenby, A. A., Viitanen, P. V., and Lorimer, G. H. (1990) Chaperonin assisted polypeptide folding and assembly. Implications for the production of functional proteins in bacteria. Trends Biotechnol. 8, 354-358
    • (1990) Trends Biotechnol. , vol.8 , pp. 354-358
    • Gatenby, A.A.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 5
    • 0026941784 scopus 로고
    • Folding and assembly of oligomeric proteins in Escherichia coli
    • Teschke, C. M., and King, J. (1992) Folding and assembly of oligomeric proteins in Escherichia coli. Curr. Opin. Biotechnol. 3, 468-473
    • (1992) Curr. Opin. Biotechnol. , vol.3 , pp. 468-473
    • Teschke, C.M.1    King, J.2
  • 6
    • 0035951410 scopus 로고    scopus 로고
    • Protein aggregation as bacterial inclusion bodies is reversible
    • DOI 10.1016/S0014-5793(01)02073-7, PII S0014579301020737
    • Carrio, M. M., and Villaverde, A. (2001) Protein aggregation as bacterial inclusion bodies is reversible. FEBS Lett. 489, 29-33 (Pubitemid 32176000)
    • (2001) FEBS Letters , vol.489 , Issue.1 , pp. 29-33
    • Carrio, M.M.1    Villaverde, A.2
  • 7
    • 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
  • 9
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • DOI 10.1016/j.jbiotec.2004.08.004, PII S0168165604004560
    • Sørensen, H. P., and Mortensen, K. K. (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115, 113-128 (Pubitemid 39656438)
    • (2005) Journal of Biotechnology , vol.115 , Issue.2 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 10
    • 13844271129 scopus 로고    scopus 로고
    • From gene to protein. A review of new and enabling technologies for multi-parallel protein expression
    • Hunt, I. (2005) From gene to protein. A review of new and enabling technologies for multi-parallel protein expression. Protein Expr. Purif. 40, 1-22
    • (2005) Protein Expr. Purif. , vol.40 , pp. 1-22
    • Hunt, I.1
  • 11
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • Ventura, S., and Villaverde, A. (2006) Protein quality in bacterial inclusion bodies. Trends Biotechnol. 24, 179-185
    • (2006) Trends Biotechnol. , vol.24 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 12
    • 10044252090 scopus 로고    scopus 로고
    • Protein folding, misfolding, and aggregation. Formation of inclusion bodies and aggresomes
    • Markossian, K. A., and Kurganov, B. I. (2004) Protein folding, misfolding, and aggregation. Formation of inclusion bodies and aggresomes. Biochemistry 69, 971-984
    • (2004) Biochemistry , vol.69 , pp. 971-984
    • Markossian, K.A.1    Kurganov, B.I.2
  • 13
    • 84863340054 scopus 로고    scopus 로고
    • Protein folding by computer: Flow far have we gone?
    • Lei, H. X., and Duan, Y. (2011) Protein folding by computer: flow far have we gone? Acta Biophys. Sin. 27, 187-194
    • (2011) Acta Biophys. Sin. , vol.27 , pp. 187-194
    • Lei, H.X.1    Duan, Y.2
  • 15
    • 14744269790 scopus 로고
    • Structure and morphology of protein inclusion bodies in Escherichia coli
    • Bowden, G. A., Paredes, A. M., and Georgiou, G. (1991) Structure and morphology of protein inclusion bodies in Escherichia coli. Biotechnology 9, 725-730
    • (1991) Biotechnology , vol.9 , pp. 725-730
    • Bowden, G.A.1    Paredes, A.M.2    Georgiou, G.3
  • 16
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
    • Speed, M. A., Wang, D. I., and King, J. (1996) Specific aggregation of partially folded polypeptide chains. The molecular basis of inclusion body composition. Nat. Biotechnol. 14, 1283-1287 (Pubitemid 26332791)
    • (1996) Nature Biotechnology , vol.14 , Issue.10 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.C.2    King, J.3
  • 17
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation. Folding aggregates, inclusion bodies and amyloid
    • Fink, A. L. (1998) Protein aggregation. Folding aggregates, inclusion bodies and amyloid. Fold Des. 3, R9-R23
    • (1998) Fold Des. , vol.3
    • Fink, A.L.1
  • 18
    • 20444363444 scopus 로고    scopus 로고
    • Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    • DOI 10.1016/j.febslet.2005.04.085, PII S0014579305006174
    • Ami, D., Natalello, A., Gatti-Lafranconi, P., Lotti, M., and Doglia, S. M. (2005) Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy. FEBS Lett. 579, 3433-3436 (Pubitemid 40800294)
    • (2005) FEBS Letters , vol.579 , Issue.16 , pp. 3433-3436
    • Ami, D.1    Natalello, A.2    Gatti-Lafranconi, P.3    Lotti, M.4    Doglia, S.M.5
  • 20
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R. (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524-530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 21
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. (2003) Protein folding and misfolding. Nature 426, 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 22
    • 79953170240 scopus 로고    scopus 로고
    • Amyloid and Alzheimer's disease
    • Lei, H. (2010) Amyloid and Alzheimer's disease. Protein Cell 1, 312-314
    • (2010) Protein Cell , vol.1 , pp. 312-314
    • Lei, H.1
  • 23
    • 0025753565 scopus 로고
    • Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli
    • Strandberg, L., and Enfors, S. O. (1991) Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli. Appl. Environ. Microbiol. 57, 1669-1674
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1669-1674
    • Strandberg, L.1    Enfors, S.O.2
  • 24
    • 14744278850 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • Wilkinson, D. L., and Harrison, R. G. (1991) Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology 9, 443-448
    • (1991) Biotechnology , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 25
    • 19944371191 scopus 로고    scopus 로고
    • Folding of a misfolding-prone β-galactosidase in absence of DnaK
    • DOI 10.1002/bit.20496
    • García-Fruitós, E., Carrió, M. M., Arís, A., and Villaverde, A. (2005) Folding of a misfolding-prone β-galactosidase in absence of DnaK. Biotechnol. Bioeng. 90, 869-875 (Pubitemid 40756681)
    • (2005) Biotechnology and Bioengineering , vol.90 , Issue.7 , pp. 869-875
    • Garcia-Fruitos, E.1    Carrio, M.M.2    Aris, A.3    Villaverde, A.4
  • 27
    • 0029778882 scopus 로고    scopus 로고
    • Linear correlation between bacterial overexpression of recombinant peptides and cell light scatter
    • Lavergne-Mazeau, F., Maftah, A., Cenatiempo, Y., and Julien, R. (1996) Linear correlation between bacterial overexpression of recombinant peptides and cell light scatter. Appl. Environ. Microbiol. 62, 3042-3046 (Pubitemid 26260123)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.8 , pp. 3042-3046
    • Lavergne-Mazeau, F.1    Maftah, A.2    Cenatiempo, Y.3    Julien, R.4
  • 28
    • 0037186259 scopus 로고    scopus 로고
    • Flow cytometry as a useful tool for process development: Rapid evaluation of expression systems
    • DOI 10.1016/S0168-1656(01)00399-6, PII S0168165601003996
    • Patkar, A., Vijayasankaran, N., Urry, D. W., and Srienc, F. (2002) Flow cytometry as a useful tool for process development. Rapid evaluation of expression systems. J. Biotechnol. 93, 217-229 (Pubitemid 34086944)
    • (2002) Journal of Biotechnology , vol.93 , Issue.3 , pp. 217-229
    • Patkar, A.1    Vijayasankaran, N.2    Urry, D.W.3    Srienc, F.4
  • 29
    • 0037454683 scopus 로고    scopus 로고
    • Coupling of chemical extraction and expanded-bed adsorption for simplified inclusion-body processing: Optimization using surface plasmon resonance
    • DOI 10.1002/bit.10471
    • Choe, W. S., Clemmitt, R. H., Chase, H. A., and Middelberg, A. P. (2003) Coupling of chemical extraction and expanded-bed adsorption for simplified inclusion-body processing. Optimization using surface plasmon resonance. Biotechnol. Bioeng. 81, 221-232 (Pubitemid 36077298)
    • (2003) Biotechnology and Bioengineering , vol.81 , Issue.2 , pp. 221-232
    • Choe, W.-S.1    Clemmitt, R.H.2    Chase, H.A.3    Middelberg, A.P.J.4
  • 30
    • 24044436165 scopus 로고    scopus 로고
    • A novel flow cytometry-based method for analysis of expression levels in Escherichia coli, giving information about precipitated and soluble protein
    • DOI 10.1016/j.jbiotec.2005.03.024, PII S0168165605001495
    • Hedhammar, M., Stenvall, M., Lönneborg, R., Nord, O., Sjölin, O., Brismar, H., Uhlén, M., Ottosson, J., and Hober, S. (2005) A novel flow cytometry- based method for analysis of expression levels in Escherichia coli, giving information about precipitated and soluble protein. J. Biotechnol. 119, 133-146 (Pubitemid 41219542)
    • (2005) Journal of Biotechnology , vol.119 , Issue.2 , pp. 133-146
    • Hedhammar, M.1    Stenvall, M.2    Lonneborg, R.3    Nord, O.4    Sjolin, O.5    Brismar, H.6    Uhlen, M.7    Ottosson, J.8    Hober, S.9
  • 32
    • 0028173464 scopus 로고
    • 12-FDG as substrates for β-galactosidase detection by flow cytometry in animal, bacterial, and yeast cells
    • Plovins, A., Alvarez, A. M., Ibañez, M., Molina, M., and Nombela, C. (1994) Use of fluorescein-di-β-D-galactopyranoside (FDG) and C12-FDG as substrates for β-galactosidase detection by flow cytometry in animal, bacterial, and yeast cells. Appl. Environ. Microbiol. 60, 4638-4641 (Pubitemid 24370848)
    • (1994) Applied and Environmental Microbiology , vol.60 , Issue.12 , pp. 4638-4641
    • Plovins, A.1    Alvarez, A.M.2    Ibanez, M.3    Molina, M.4    Nombela, C.5
  • 35
    • 0034616258 scopus 로고    scopus 로고
    • Fine architecture of bacterial inclusion bodies
    • DOI 10.1016/S0014-5793(00)01357-0, PII S0014579300013570
    • Carrió, M. M., Cubarsi, R., and Villaverde, A. (2000) Fine architecture of bacterial inclusion bodies. FEBS Lett. 471, 7-11 (Pubitemid 30173283)
    • (2000) FEBS Letters , vol.471 , Issue.1 , pp. 7-11
    • Carrio, M.M.1    Cubarsi, R.2    Villaverde, A.3
  • 36
    • 18244398660 scopus 로고    scopus 로고
    • Localization of chaperones DnaK and GroEL in bacterial inclusion bodies
    • DOI 10.1128/JB.187.10.3599-3601.2005
    • Carrió, M. M., and Villaverde, A. (2005) Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J. Bacteriol. 187, 3599-3601 (Pubitemid 40628721)
    • (2005) Journal of Bacteriology , vol.187 , Issue.10 , pp. 3599-3601
    • Carrio, M.M.1    Villaverde, A.2


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