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Volumn 91, Issue 4, 2011, Pages 1203-1213

Simple defined autoinduction medium for high-level recombinant protein production using T7-based Escherichia coli expression systems

Author keywords

Autoinduction; Defined medium; Escherichia coli; Recombinant protein production

Indexed keywords

96-WELL MICROTITER PLATE; AUTOINDUCTION; AVERAGE YIELD; CARBON SUBSTRATES; DEFINED MEDIUM; DIAUXIC GROWTH; E. COLI; ESCHERICHIA COLI EXPRESSION SYSTEMS; EXPRESSION SYSTEM; LAC OPERON; LURIA-BERTANI BROTHS; NITROGEN SOURCES; PROTEIN CONCENTRATIONS; PROTEIN PRODUCTION; RECOMBINANT PROTEIN PRODUCTIONS; REGULATORY ELEMENTS; SHAKE FLASKS; TARGET PROTEINS; TEST TUBE;

EID: 80052628175     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3407-z     Document Type: Article
Times cited : (82)

References (31)
  • 1
    • 0030460083 scopus 로고    scopus 로고
    • Quantitative measurement of green fluorescent protein expression
    • CR Albano L Randers-Eichhorn Q Chang WR Bentley G Rao 1996 Quantitative measurement of green fluorescent protein expression Biotechnol Tech 10 953 958 10.1007/BF00180401 10.1007/BF00180401 1:CAS:528:DyaK2sXhtlGgtQ%3D%3D (Pubitemid 27025348)
    • (1996) Biotechnology Techniques , vol.10 , Issue.12 , pp. 953-958
    • Albano, C.R.1    Randers-Eichhon, L.2    Chang, Q.3    Bentley, W.E.4    Rao, G.5
  • 2
    • 57649158626 scopus 로고    scopus 로고
    • Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain
    • 10.1074/jbc.M804746200 10.1074/jbc.M804746200 1:CAS:528: DC%2BD1cXht1yntL7P
    • E Bitto CA Bingman L Bittova DA Kondrashov RM Bannen BG Fox JL Markley GN Phillips Jr. 2008 Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain J Biol Chem 283 30184 30192 10.1074/jbc.M804746200 10.1074/jbc.M804746200 1:CAS:528:DC%2BD1cXht1yntL7P
    • (2008) J Biol Chem , vol.283 , pp. 30184-30192
    • Bitto, E.1    Bingman, C.A.2    Bittova, L.3    Kondrashov, D.A.4    Bannen, R.M.5    Fox, B.G.6    Markley, J.L.7    Phillips Jr., G.N.8
  • 3
    • 67650230364 scopus 로고    scopus 로고
    • X-ray structure of Danio rerio secretagogin: A hexa-EF-hand calcium sensor
    • 10.1002/prot.22362 10.1002/prot.22362 1:CAS:528:DC%2BD1MXntlehtb8%3D
    • E Bitto CA Bingman L Bittova RO Frederick BG Fox GN Phillips Jr. 2009 X-ray structure of Danio rerio secretagogin: a hexa-EF-hand calcium sensor Proteins Struct Funct Bioinf 76 477 483 10.1002/prot.22362 10.1002/prot.22362 1:CAS:528:DC%2BD1MXntlehtb8%3D
    • (2009) Proteins Struct Funct Bioinf , vol.76 , pp. 477-483
    • Bitto, E.1    Bingman, C.A.2    Bittova, L.3    Frederick, R.O.4    Fox, B.G.5    Phillips Jr., G.N.6
  • 4
    • 34250316620 scopus 로고    scopus 로고
    • Enhanced bacterial protein expression during auto-induction obtained by alteration of lac repressor dosage and medium composition
    • DOI 10.1021/bp070011x
    • PG Blommel KJ Becker P Duvnjak BG Fox 2007 Enhanced bacterial protein expression during auto-induction obtained by alteration of lac repressor dosage and medium composition Biotechnol Prog 23 585 598 10.1021/bp070011x 10.1021/bp070011x 1:CAS:528:DC%2BD2sXlt1ylt7s%3D (Pubitemid 46911182)
    • (2007) Biotechnology Progress , vol.23 , Issue.3 , pp. 585-598
    • Blommel, P.G.1    Becker, K.J.2    Duvnjak, P.3    Fox, B.G.4
  • 6
    • 62449111582 scopus 로고    scopus 로고
    • Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidoglycan hydrolase of Listeria monocytogenes
    • 10.1111/j.1365-2958.2009.06619.x 10.1111/j.1365-2958.2009.06619.x 1:CAS:528:DC%2BD1MXktVWhsLo%3D
    • M Bublitz L Polle C Holland DW Heinz M Nimtz WD Schubert 2009 Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidoglycan hydrolase of Listeria monocytogenes Mol Microbiol 71 1509 1522 10.1111/j.1365-2958.2009.06619.x 10.1111/j.1365-2958.2009.06619.x 1:CAS:528:DC%2BD1MXktVWhsLo%3D
    • (2009) Mol Microbiol , vol.71 , pp. 1509-1522
    • Bublitz, M.1    Polle, L.2    Holland, C.3    Heinz, D.W.4    Nimtz, M.5    Schubert, W.D.6
  • 7
  • 8
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • M Chalfie Y Tu G Euskirchen WW Ward DC Prasher 1994 Green fluorescent protein as a marker for gene expression Science 263 802 805 10.1126/science. 8303295 10.1126/science.8303295 1:CAS:528:DyaK2cXitFWkurc%3D (Pubitemid 24093206)
    • (1994) Science , vol.263 , Issue.5148 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 9
    • 0035431321 scopus 로고    scopus 로고
    • Structure of the PPARα and -γ ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family
    • DOI 10.1016/S0969-2126(01)00634-7, PII S0969212601006347
    • P Cronet JF Petersen R Folmer N Blomberg K Sjoblom U Karlsson EL Lindstedt K Bamberg 2001 Structure of the PPARα and -γ ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family Structure 9 699 706 10.1016/S0969-2126(01)00634-7 10.1016/S0969-2126(01)00634-7 1:CAS:528:DC%2BD3MXmtV2ku78%3D (Pubitemid 32772892)
    • (2001) Structure , vol.9 , Issue.8 , pp. 699-706
    • Cronet, P.1    Petersen, J.F.W.2    Folmer, R.3    Blomberg, N.4    Sjoblom, K.5    Karlsson, U.6    Lindstedt, E.-L.7    Bamberg, K.8
  • 11
    • 65249138782 scopus 로고    scopus 로고
    • Autoinduction of protein expression
    • doi: 10.1002/0471140864.ps0523s56
    • Fox BG, Blommel PG (2009) Autoinduction of protein expression. Curr Protoc Protein Sci Chapter 5:Unit 5.23. doi: 10.1002/0471140864.ps0523s56
    • (2009) Curr Protoc Protein Sci Chapter 5:Unit , vol.5 , pp. 23
    • Fox, B.G.1    Blommel, P.G.2
  • 13
    • 0034518308 scopus 로고    scopus 로고
    • Kinetics of heat-shock response and inclusion body formation during temperature-induced production of basic fibroblast growth factor in high-cell-density cultures of recombinant Escherichia coli
    • DOI 10.1021/bp0000959
    • F Hoffmann U Rinas 2000 Kinetics of heat-shock response and inclusion body formation during temperature-induced production of basic fibroblast growth factor in high-cell-density cultures of recombinant Escherichia coli Biotechnol Prog 16 1000 1007 10.1021/bp0000959 10.1021/bp0000959 1:CAS:528: DC%2BD3cXntVehtbk%3D (Pubitemid 32044852)
    • (2000) Biotechnology Progress , vol.16 , Issue.6 , pp. 1000-1007
    • Hoffmann, F.1    Rinas, U.2
  • 14
    • 0442292087 scopus 로고    scopus 로고
    • Minimizing inclusion body formation during recombinant protein production in Escherichia coli at bench and pilot plant scale
    • DOI 10.1016/j.enzmictec.2003.10.011
    • F Hoffmann J van den Heuvel N Zidek U Rinas 2004 Minimizing inclusion body formation during recombinant protein production in Escherichia coli at bench and pilot plant scale Enzyme Microb Technol 34 235 241 10.1016/j.enzmictec.2003.10.011 10.1016/j.enzmictec.2003.10.011 1:CAS:528:DC%2BD2cXhtFWnt7Y%3D (Pubitemid 38186729)
    • (2004) Enzyme and Microbial Technology , vol.34 , Issue.3-4 , pp. 235-241
    • Hoffmann, F.1    Van Den Heuvel, J.2    Zidek, N.3    Rinas, U.4
  • 15
    • 0004212736 scopus 로고
    • Composition, organization, and structure of the bacterial cell
    • Sinauer Associates Inc, Sunderland
    • Ingraham JL, Maaloe O, Neidhardt FC (1983) Composition, organization, and structure of the bacterial cell. In: Growth of the bacterial cell. Sinauer Associates Inc, Sunderland, pp 1-48
    • (1983) Growth of the Bacterial Cell , pp. 1-48
    • Ingraham, J.L.1    Maaloe, O.2    Neidhardt, F.C.3
  • 16
    • 15844371174 scopus 로고    scopus 로고
    • Metabolic flux analysis of Escherichia coli in glucose-limited continuous culture. I. Growth-rate-dependent metabolic efficiency at steady state
    • DOI 10.1099/mic.0.27481-0
    • A Kayser J Weber V Hecht U Rinas 2005 Metabolic flux analysis of Escherichia coli in glucose-limited continuous culture. I. Growth-rate-dependent metabolic efficiency at steady state Microbiology 151 693 706 10.1099/mic.0.27481-0 10.1099/mic.0.27481-0 1:CAS:528:DC%2BD2MXis1yqs7Y%3D (Pubitemid 40425005)
    • (2005) Microbiology , vol.151 , Issue.3 , pp. 693-706
    • Kayser, A.1    Weber, J.2    Hecht, V.3    Rinas, U.4
  • 17
    • 0029239706 scopus 로고
    • Simple fed-batch technique for high cell density cultivation of Escherichia coli
    • 10.1016/0168-1656(94)00143-Z 10.1016/0168-1656(94)00143-Z 1:CAS:528:DyaK2MXjvVemtLk%3D
    • DJ Korz U Rinas K Hellmuth EA Sanders WD Deckwer 1995 Simple fed-batch technique for high cell density cultivation of Escherichia coli J Biotechnol 39 59 65 10.1016/0168-1656(94)00143-Z 10.1016/0168-1656(94)00143-Z 1:CAS:528:DyaK2MXjvVemtLk%3D
    • (1995) J Biotechnol , vol.39 , pp. 59-65
    • Korz, D.J.1    Rinas, U.2    Hellmuth, K.3    Sanders, E.A.4    Deckwer, W.D.5
  • 18
    • 33746275230 scopus 로고    scopus 로고
    • The discovery of SycO highlights a new function for type III secretion effector chaperones
    • DOI 10.1038/sj.emboj.7601202, PII 7601202
    • M Letzelter I Sorg LJ Mota S Meyer J Stalder M Feldman M Kuhn I Callebaut GR Cornelis 2006 The discovery of SycO highlights a new function for type III secretion effector chaperones EMBO J 25 3223 3233 10.1038/sj.emboj.7601202 10.1038/sj.emboj.7601202 1:CAS:528:DC%2BD28XmvFajurY%3D (Pubitemid 44106772)
    • (2006) EMBO Journal , vol.25 , Issue.13 , pp. 3223-3233
    • Letzelter, M.1    Sorg, I.2    Mota, L.J.3    Meyer, S.4    Stalder, J.5    Feldman, M.6    Kuhn, M.7    Callebaut, I.8    Cornelis, G.R.9
  • 19
    • 84889234826 scopus 로고    scopus 로고
    • Targeting of Host Rab GTPase Function by the Intravacuolar Pathogen Legionella pneumophila
    • DOI 10.1016/j.devcel.2006.05.013, PII S1534580706002541
    • MP Machner RR Isberg 2006 Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila Dev Cell 11 47 56 10.1016/j.devcel.2006.05.013 10.1016/j.devcel.2006.05.013 1:CAS:528: DC%2BD28XnsVWnt78%3D (Pubitemid 43960806)
    • (2006) Developmental Cell , vol.11 , Issue.1 , pp. 47-56
    • Machner, M.P.1    Isberg, R.R.2
  • 20
    • 77956189386 scopus 로고    scopus 로고
    • Characterization of recombinant UDP-galactopyranose mutase from Aspergillus fumigatus
    • 10.1016/j.abb.2010.06.035 10.1016/j.abb.2010.06.035 1:CAS:528: DC%2BC3cXhtV2isrnJ
    • M Oppenheimer MB Poulin TL Lowary RF Helm P Sobrado 2010 Characterization of recombinant UDP-galactopyranose mutase from Aspergillus fumigatus Arch Biochem Biophys 502 31 38 10.1016/j.abb.2010.06.035 10.1016/j.abb.2010.06.035 1:CAS:528:DC%2BC3cXhtV2isrnJ
    • (2010) Arch Biochem Biophys , vol.502 , pp. 31-38
    • Oppenheimer, M.1    Poulin, M.B.2    Lowary, T.L.3    Helm, R.F.4    Sobrado, P.5
  • 21
    • 33846222898 scopus 로고    scopus 로고
    • Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli
    • DOI 10.1016/j.jbiotec.2006.07.004, PII S0168165606005888
    • U Rinas F Hoffmann E Betiku D Estape S Marten 2007 Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli J Biotechnol 127 244 257 10.1016/j.jbiotec.2006.07.004 10.1016/j.jbiotec.2006.07.004 1:CAS:528:DC%2BD28Xht1ShtL3I (Pubitemid 46107138)
    • (2007) Journal of Biotechnology , vol.127 , Issue.2 , pp. 244-257
    • Rinas, U.1    Hoffmann, F.2    Betiku, E.3    Estape, D.4    Marten, S.5
  • 23
    • 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
    • 10.1002/(SICI)1097-0290(1999)66:1<61::AID-BIT6>3.0.CO;2-G 10.1002/(SICI)1097-0290(1999)66:1<61::AID-BIT6>3.0.CO;2-G 1:CAS:528:DyaK1MXnslKqsrk%3D
    • M Schmidt E Viaplana F Hoffmann S Marten A Villaverde 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 10.1002/(SICI)1097-0290(1999) 66:1<61::AID-BIT6>3.0.CO;2-G 10.1002/(SICI)1097-0290(1999)66:1<61::AID- BIT6>3.0.CO;2-G 1:CAS:528:DyaK1MXnslKqsrk%3D
    • (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
  • 24
    • 65649135871 scopus 로고    scopus 로고
    • Practical protocols for production of very high yields of recombinant proteins using Escherichia coli
    • 10.1002/pro.102 10.1002/pro.102 1:CAS:528:DC%2BD1MXms1agsLg%3D
    • A Sivashanmugam V Murray C Cui Y Zhang J Wang Q Li 2009 Practical protocols for production of very high yields of recombinant proteins using Escherichia coli Protein Sci 18 936 948 10.1002/pro.102 10.1002/pro.102 1:CAS:528:DC%2BD1MXms1agsLg%3D
    • (2009) Protein Sci , vol.18 , pp. 936-948
    • Sivashanmugam, A.1    Murray, V.2    Cui, C.3    Zhang, Y.4    Wang, J.5    Li, Q.6
  • 25
    • 39549122212 scopus 로고    scopus 로고
    • A protein structure initiative approach to expression, purification, and in situ delivery of human cytochrome b5 to membrane vesicles
    • 10.1016/j.pep.2007.11.018 10.1016/j.pep.2007.11.018 1:CAS:528: DC%2BD1cXitlCjt7c%3D
    • P Sobrado MA Goren D James CK Amundson BG Fox 2008 A protein structure initiative approach to expression, purification, and in situ delivery of human cytochrome b5 to membrane vesicles Protein Expr Purif 58 229 241 10.1016/j.pep.2007.11.018 10.1016/j.pep.2007.11.018 1:CAS:528: DC%2BD1cXitlCjt7c%3D
    • (2008) Protein Expr Purif , vol.58 , pp. 229-241
    • Sobrado, P.1    Goren, M.A.2    James, D.3    Amundson, C.K.4    Fox, B.G.5
  • 27
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • 10.1016/j.pep.2005.01.016 10.1016/j.pep.2005.01.016 1:CAS:528: DC%2BD2MXjsFCktLw%3D
    • FW Studier 2005 Protein production by auto-induction in high density shaking cultures Protein Expr Purif 41 207 234 10.1016/j.pep.2005.01.016 10.1016/j.pep.2005.01.016 1:CAS:528:DC%2BD2MXjsFCktLw%3D
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 28
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • 10.1016/0022-2836(86)90385-2 10.1016/0022-2836(86)90385-2 1:CAS:528:DyaL28XktlKrsr4%3D
    • FW Studier BA Moffatt 1986 Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes J Mol Biol 189 113 130 10.1016/0022-2836(86)90385-2 10.1016/0022-2836(86)90385-2 1:CAS:528: DyaL28XktlKrsr4%3D
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 29
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • DOI 10.1146/annurev.biochem.67.1.509
    • RY Tsien 1998 The green fluorescent protein Annu Rev Biochem 67 509 544 10.1146/annurev.biochem.67.1.509 10.1146/annurev.biochem.67.1.509 1:CAS:528:DyaK1cXlsFOmsb8%3D (Pubitemid 28411137)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 31
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia cell and purified by high-affinity column refolding
    • DOI 10.1016/S0014-5793(97)01330-6, PII S0014579397013306
    • R Zahn C von Schroetter K Wuthrich 1997 Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding FEBS Lett 417 400 404 10.1016/S0014-5793(97)01330-6 10.1016/S0014-5793(97)01330-6 1:CAS:528:DyaK2sXnt1ekurY%3D (Pubitemid 27511631)
    • (1997) FEBS Letters , vol.417 , Issue.3 , pp. 400-404
    • Zahn, R.1    Von Schroetter, C.2    Wuthrich, K.3


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