메뉴 건너뛰기




Volumn 6, Issue , 2012, Pages

A synthetic biology approach to self-regulatory recombinant protein production in Escherichia coli

Author keywords

Escherichia coli; Recombinant protein; Self regulatory; Stress promoter; Synthetic biology

Indexed keywords

RECOMBINANT PROTEIN;

EID: 84859010199     PISSN: None     EISSN: 17541611     Source Type: Journal    
DOI: 10.1186/1754-1611-6-2     Document Type: Article
Times cited : (43)

References (30)
  • 2
    • 33750587201 scopus 로고    scopus 로고
    • Manufacturing of recombinant therapeutic proteins in microbial systems
    • 10.1002/biot.200500051, 16892246
    • Graumann K, Premstaller A. Manufacturing of recombinant therapeutic proteins in microbial systems. Biotechnol J 2006, 1:164-186. 10.1002/biot.200500051, 16892246.
    • (2006) Biotechnol J , vol.1 , pp. 164-186
    • Graumann, K.1    Premstaller, A.2
  • 3
    • 33846126638 scopus 로고    scopus 로고
    • Antibody production with yeasts and filamentous fungi: on the road to large scale?
    • Gasser B, Mattanovich D. Antibody production with yeasts and filamentous fungi: on the road to large scale?. BiotechnolLett 2007, 29:201-212.
    • (2007) BiotechnolLett , vol.29 , pp. 201-212
    • Gasser, B.1    Mattanovich, D.2
  • 4
    • 61349178501 scopus 로고    scopus 로고
    • Production of recombinant proteins by microbes and higher organisms
    • Vaishnav P. Production of recombinant proteins by microbes and higher organisms. BiotechnolAdv 2009, 27:297-306.
    • (2009) BiotechnolAdv , vol.27 , pp. 297-306
    • Vaishnav, P.1
  • 5
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: the advent of fully humanized yeast
    • Hamilton S, Gerngross T. Glycosylation engineering in yeast: the advent of fully humanized yeast. CurrOpinBiotechnol 2007, 18:387-392.
    • (2007) CurrOpinBiotechnol , vol.18 , pp. 387-392
    • Hamilton, S.1    Gerngross, T.2
  • 6
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • 10.1038/nbt1029, 15529165
    • Baneyx F, Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 2004, 22:1399-1408. 10.1038/nbt1029, 15529165.
    • (2004) Nat Biotechnol , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 9
    • 0033672578 scopus 로고    scopus 로고
    • A comparative study of global stress gene regulation in response to overexpression of recombinant proteins in Escherichia coli
    • Gill R, Valdes J, Bentley W. A comparative study of global stress gene regulation in response to overexpression of recombinant proteins in Escherichia coli. MetabEng 2000, 2:178-189.
    • (2000) MetabEng , vol.2 , pp. 178-189
    • Gill, R.1    Valdes, J.2    Bentley, W.3
  • 10
    • 0026784986 scopus 로고
    • Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
    • 207373, 1356969
    • Allen S, Polazzi J, Gierse J, Easton A. Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli. J Bacteriol 1992, 174:6938-6947. 207373, 1356969.
    • (1992) J Bacteriol , vol.174 , pp. 6938-6947
    • Allen, S.1    Polazzi, J.2    Gierse, J.3    Easton, A.4
  • 12
    • 39649109246 scopus 로고    scopus 로고
    • A crosslinked inclusion body process for sialic acid synthesis
    • 10.1016/j.jbiotec.2008.01.014, 18313163
    • Nahálka J, Vikartovská A, Hrabárová E. A crosslinked inclusion body process for sialic acid synthesis. J Biotechnol 2008, 134:146-153. 10.1016/j.jbiotec.2008.01.014, 18313163.
    • (2008) J Biotechnol , vol.134 , pp. 146-153
    • Nahálka, J.1    Vikartovská, A.2    Hrabárová, E.3
  • 13
    • 34548508428 scopus 로고    scopus 로고
    • Production of recombinant proteins in Bacillus subtilis
    • Schumann W. Production of recombinant proteins in Bacillus subtilis. AdvApplMicrobiol 2007, 62:137-189.
    • (2007) AdvApplMicrobiol , vol.62 , pp. 137-189
    • Schumann, W.1
  • 14
    • 18844362113 scopus 로고    scopus 로고
    • Strategies for efficient production of heterologous proteins in Escherichia coli
    • Jana S, Deb J. Strategies for efficient production of heterologous proteins in Escherichia coli. ApplMicrobiolBiotechnol 2005, 67:289-298.
    • (2005) ApplMicrobiolBiotechnol , vol.67 , pp. 289-298
    • Jana, S.1    Deb, J.2
  • 16
    • 4444320606 scopus 로고    scopus 로고
    • A high-copy T7 Escherichia coli expression vector for the production of recombinant proteins with a minimal N-terminal His-tagged fusion peptide
    • Ramos CR, Abreu PA, Nascimento AL, Ho PL. A high-copy T7 Escherichia coli expression vector for the production of recombinant proteins with a minimal N-terminal His-tagged fusion peptide. Braz J Med Biol Res 2004, 37:1103-1109.
    • (2004) Braz J Med Biol Res , vol.37 , pp. 1103-1109
    • Ramos, C.R.1    Abreu, P.A.2    Nascimento, A.L.3    Ho, P.L.4
  • 17
    • 0027445907 scopus 로고
    • Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
    • 10.1016/0378-1119(93)90167-2, 8244018
    • Chuang S, Burland V, Plunkett G, Daniels D, Blattner F. Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. Gene 1993, 134:1-6. 10.1016/0378-1119(93)90167-2, 8244018.
    • (1993) Gene , vol.134 , pp. 1-6
    • Chuang, S.1    Burland, V.2    Plunkett, G.3    Daniels, D.4    Blattner, F.5
  • 18
    • 43049096460 scopus 로고    scopus 로고
    • Monitoring of transcriptome and proteome profiles to investigate the cellular response of E. coli towards recombinant protein expression under defined chemostat conditions
    • 10.1016/j.jbiotec.2008.02.013, 18405993
    • Dürrschmid K, Reischer H, Schmidt-Heck W, Hrebicek T, Guthke R, Rizzi A, Bayer K. Monitoring of transcriptome and proteome profiles to investigate the cellular response of E. coli towards recombinant protein expression under defined chemostat conditions. J Biotechnol 2008, 135:34-44. 10.1016/j.jbiotec.2008.02.013, 18405993.
    • (2008) J Biotechnol , vol.135 , pp. 34-44
    • Dürrschmid, K.1    Reischer, H.2    Schmidt-Heck, W.3    Hrebicek, T.4    Guthke, R.5    Rizzi, A.6    Bayer, K.7
  • 19
    • 0036213467 scopus 로고    scopus 로고
    • Gene expression response to misfolded protein as a screen for soluble recombinant protein
    • 10.1093/protein/15.2.153, 11917152
    • Lesley S, Graziano J, Cho C, Knuth M, Klock H. Gene expression response to misfolded protein as a screen for soluble recombinant protein. Protein Eng 2002, 15:153-160. 10.1093/protein/15.2.153, 11917152.
    • (2002) Protein Eng , vol.15 , pp. 153-160
    • Lesley, S.1    Graziano, J.2    Cho, C.3    Knuth, M.4    Klock, H.5
  • 20
    • 0043031143 scopus 로고    scopus 로고
    • Enhanced production of insulin-like growth factor I fusion protein in Escherichia coli by coexpression of the down-regulated genes identified by transcriptome profiling
    • 10.1128/AEM.69.8.4737-4742.2003, 169106, 12902266
    • Choi J, Lee S, Lee S. Enhanced production of insulin-like growth factor I fusion protein in Escherichia coli by coexpression of the down-regulated genes identified by transcriptome profiling. Appl Environ Microbiol 2003, 69:4737-4742. 10.1128/AEM.69.8.4737-4742.2003, 169106, 12902266.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 4737-4742
    • Choi, J.1    Lee, S.2    Lee, S.3
  • 21
    • 0034693456 scopus 로고    scopus 로고
    • Monitoring of genes that respond to overproduction of an insoluble recombinant protein in Escherichia coli glucose-limited fed-batch fermentations
    • Jürgen B, Lin H, Riemschneider S, Scharf C, Neubauer P, Schmid R, Hecker M, Schweder T. Monitoring of genes that respond to overproduction of an insoluble recombinant protein in Escherichia coli glucose-limited fed-batch fermentations. BiotechnolBioeng 2000, 70:217-224.
    • (2000) BiotechnolBioeng , vol.70 , pp. 217-224
    • Jürgen, B.1    Lin, H.2    Riemschneider, S.3    Scharf, C.4    Neubauer, P.5    Schmid, R.6    Hecker, M.7    Schweder, T.8
  • 22
    • 0034087676 scopus 로고    scopus 로고
    • Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system
    • Orth P, Schnappinger D, Hillen W, Saenger W, Hinrichs W. Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system. Nat StructBiol 2000, 7:215-219.
    • (2000) Nat StructBiol , vol.7 , pp. 215-219
    • Orth, P.1    Schnappinger, D.2    Hillen, W.3    Saenger, W.4    Hinrichs, W.5
  • 23
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • 10.1016/S1097-2765(00)80243-9, 10882100
    • Kim Y, Burton R, Burton B, Sauer R, Baker T. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol Cell 2000, 5:639-648. 10.1016/S1097-2765(00)80243-9, 10882100.
    • (2000) Mol Cell , vol.5 , pp. 639-648
    • Kim, Y.1    Burton, R.2    Burton, B.3    Sauer, R.4    Baker, T.5
  • 24
    • 57049159362 scopus 로고    scopus 로고
    • A fast, robust and tunable synthetic gene oscillator
    • 10.1038/nature07389, 18971928
    • Stricker J, Cookson S, Bennett M, Mather W, Tsimring L, Hasty J. A fast, robust and tunable synthetic gene oscillator. Nature 2008, 456:516-519. 10.1038/nature07389, 18971928.
    • (2008) Nature , vol.456 , pp. 516-519
    • Stricker, J.1    Cookson, S.2    Bennett, M.3    Mather, W.4    Tsimring, L.5    Hasty, J.6
  • 25
    • 0034688173 scopus 로고    scopus 로고
    • A synthetic oscillatory network of transcriptional regulators
    • 10.1038/35002125, 10659856
    • Elowitz MB, Leibler S. A synthetic oscillatory network of transcriptional regulators. Nature 2000, 403:335-338. 10.1038/35002125, 10659856.
    • (2000) Nature , vol.403 , pp. 335-338
    • Elowitz, M.B.1    Leibler, S.2
  • 26
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • 10.1016/0378-1119(95)00685-0, 8707053
    • Cormack BP, Valdivia RH, Falkow S. FACS-optimized mutants of the green fluorescent protein (GFP). Gene 1996, 173:33-38. 10.1016/0378-1119(95)00685-0, 8707053.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 27
    • 34648828365 scopus 로고    scopus 로고
    • Directed evolution of AraC for improved compatibility of arabinose- and lactose-inducible promoters
    • 10.1128/AEM.00791-07, 2074931, 17644634
    • Lee S, Chou H, Pfleger B, Newman J, Yoshikuni Y, Keasling J. Directed evolution of AraC for improved compatibility of arabinose- and lactose-inducible promoters. Appl Environ Microbiol 2007, 73:5711-5715. 10.1128/AEM.00791-07, 2074931, 17644634.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 5711-5715
    • Lee, S.1    Chou, H.2    Pfleger, B.3    Newman, J.4    Yoshikuni, Y.5    Keasling, J.6
  • 28
    • 85027918827 scopus 로고    scopus 로고
    • Enzyme characteristics of aminotransferase FumI of Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B(1)
    • Hartinger D, Schwartz H, Hametner C, Schatzmayr G, Haltrich D, Moll WD. Enzyme characteristics of aminotransferase FumI of Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B(1). ApplMicrobiolBiotechnol 2011, 91(3):757-68.
    • (2011) ApplMicrobiolBiotechnol , vol.91 , Issue.3 , pp. 757-768
    • Hartinger, D.1    Schwartz, H.2    Hametner, C.3    Schatzmayr, G.4    Haltrich, D.5    Moll, W.D.6
  • 29
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B, Walker JE. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J MolBiol 1996, 260:289-298.
    • (1996) J MolBiol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 30
    • 0023198428 scopus 로고
    • Kinetic analysis of T7 RNA polymerase-promoter interactions with small synthetic promoters
    • 10.1021/bi00384a006, 3300768
    • Martin CT, Coleman JE. Kinetic analysis of T7 RNA polymerase-promoter interactions with small synthetic promoters. Biochemistry 1987, 26:2690-2696. 10.1021/bi00384a006, 3300768.
    • (1987) Biochemistry , vol.26 , pp. 2690-2696
    • Martin, C.T.1    Coleman, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.