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Volumn 97, Issue 2, 2013, Pages 837-845

A simple and effective strategy for solving the problem of inclusion bodies in recombinant protein technology: His-tag deletions enhance soluble expression

Author keywords

(+) Lactamase; ( ) Lactamase; His tag; Inclusion bodies; Uridine phosphorylase

Indexed keywords

AEROPYRUM PERNIX; BRADYRHIZOBIUM JAPONICUM; E. COLI; FUSION PARTNERS; FUSION TAG; HETEROLOGOUS PROTEINS; HIS-TAG; INCLUSION BODIES; INTENSIVE RESEARCH; KEY FACTORS; LACTAMASES; MICROBIAL CELL FACTORIES; PET SYSTEMS; POWERFUL SYSTEMS; PROCESS NEEDS; PRODUCTION OF; PROTEIN EXPRESSIONS; SOLUBLE EXPRESSION; STRUCTURE-BASED; TARGET PROTEINS; URIDINE PHOSPHORYLASE;

EID: 84873996574     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4630-y     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 0037022657 scopus 로고    scopus 로고
    • Proteome-scale purification of human proteins from bacteria
    • 10.1073/pnas.042684199 10.1073/pnas.042684199 1:CAS:528: DC%2BD38Xit1Crsb0%3D
    • Braun P, Hu Y, Shen B, Halleck A, Koundinya M, Harlow E, LaBaer J (2002) Proteome-scale purification of human proteins from bacteria. P Natl Acad Sci 99(5):2654-2659. doi: 10.1073/pnas.042684199
    • (2002) P Natl Acad Sci , vol.99 , Issue.5 , pp. 2654-2659
    • Braun, P.1    Hu, Y.2    Shen, B.3    Halleck, A.4    Koundinya, M.5    Harlow, E.6    Labaer, J.7
  • 3
    • 0037468523 scopus 로고    scopus 로고
    • Role of molecular chaperones in inclusion body formation
    • 10.1016/S0014-5793(03)00126-1
    • Carrió MM, Villaverde A (2003) Role of molecular chaperones in inclusion body formation. FEBS Lett 537(1-3):215-221
    • (2003) FEBS Lett , vol.537 , Issue.1-3 , pp. 215-221
    • Carrió, M.M.1    Villaverde, A.2
  • 4
    • 0034616258 scopus 로고    scopus 로고
    • Fine architecture of bacterial inclusion bodies
    • 10.1016/S0014-5793(00)01357-0
    • Carrió MM, Cubarsi R, Villaverde A (2000) Fine architecture of bacterial inclusion bodies. FEBS Lett 471(1):7-11
    • (2000) FEBS Lett , vol.471 , Issue.1 , pp. 7-11
    • Carrió, M.M.1    Cubarsi, R.2    Villaverde, A.3
  • 5
    • 57149092786 scopus 로고    scopus 로고
    • Identification of Mycobacterium tuberculosis vaccine candidates using human CD4+ T-cells expression cloning
    • 10.1016/j.vaccine.2008.10.056 1:CAS:528:DC%2BD1cXhsV2gurfE
    • Coler RN, Dillon DC, Skeiky YAW, Kahn M, Orme IM, Lobet Y, Reed SG, Alderson MR (2009) Identification of Mycobacterium tuberculosis vaccine candidates using human CD4+ T-cells expression cloning. Vaccine 27(2):223-233
    • (2009) Vaccine , vol.27 , Issue.2 , pp. 223-233
    • Coler, R.N.1    Dillon, D.C.2    Skeiky, Y.A.W.3    Kahn, M.4    Orme, I.M.5    Lobet, Y.6    Reed, S.G.7    Alderson, M.R.8
  • 6
    • 84862287074 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of an insoluble glucan-producing glucansucrase from Leuconostoc mesenteroides NRRL B-1118
    • 10.1007/s00253-011-3562-2 10.1007/s00253-011-3562-2
    • Côté G, Skory C (2011) Cloning, expression, and characterization of an insoluble glucan-producing glucansucrase from Leuconostoc mesenteroides NRRL B-1118. Appl Microbiol Biot 93(6):2387-2394. doi: 10.1007/s00253-011-3562-2
    • (2011) Appl Microbiol Biot , vol.93 , Issue.6 , pp. 2387-2394
    • Côté, G.1    Skory, C.2
  • 7
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • 10.1016/S0958-1669(98)80109-2
    • De Bernardez CE (1998) Refolding of recombinant proteins. Curr Opin Biotech 9(2):157-163
    • (1998) Curr Opin Biotech , vol.9 , Issue.2 , pp. 157-163
    • De Bernardez, C.E.1
  • 8
    • 33750991319 scopus 로고    scopus 로고
    • Effect of temperature on protein quality in bacterial inclusion bodies
    • 10.1016/j.febslet.2006.10.071
    • de Groot NS, Ventura S (2006) Effect of temperature on protein quality in bacterial inclusion bodies. FEBS Lett 580(27):6471-6476
    • (2006) FEBS Lett , vol.580 , Issue.27 , pp. 6471-6476
    • De Groot, N.S.1    Ventura, S.2
  • 9
    • 48649087458 scopus 로고    scopus 로고
    • Studies on bacterial inclusion bodies
    • 10.2217/17460913.3.4.423 10.2217/17460913.3.4.423
    • de Groot NS, Espargaró A, More M, Ventura S (2008) Studies on bacterial inclusion bodies. Future Microbiol 3(4):423-435. doi: 10.2217/17460913.3.4.423
    • (2008) Future Microbiol , vol.3 , Issue.4 , pp. 423-435
    • De Groot, N.S.1    Espargaró, A.2    More, M.3    Ventura, S.4
  • 10
    • 83455237063 scopus 로고    scopus 로고
    • Morphological and physiological response of soybean treated with the microsymbiont Bradyrhizobium japonicum pre-incubated with genistein
    • 10.1016/j.sajb.2011.11.001
    • Dolatabadian A, Sanavy SAMM, Ghanati F, Gresshoff PM (2012) Morphological and physiological response of soybean treated with the microsymbiont Bradyrhizobium japonicum pre-incubated with genistein. S Afr J Bot 79:9-18
    • (2012) S Afr J Bot , vol.79 , pp. 9-18
    • Dolatabadian, A.1    Sanavy, S.2    Ghanati, F.3    Gresshoff, P.M.4
  • 11
    • 0027908939 scopus 로고
    • Isolation, renaturation, and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies
    • 10.1002/bit.260410103 10.1002/bit.260410103 1:CAS:528: DyaK3sXnvFersw%3D%3D
    • Fischer B, Sumner I, Goodenough P (1993) Isolation, renaturation, and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies. Biotechnol Bioeng 41(1):3-13. doi: 10.1002/bit.260410103
    • (1993) Biotechnol Bioeng , vol.41 , Issue.1 , pp. 3-13
    • Fischer, B.1    Sumner, I.2    Goodenough, P.3
  • 13
    • 79959952063 scopus 로고    scopus 로고
    • Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology
    • 10.1111/j.1742-4658.2011.08163.x 10.1111/j.1742-4658.2011.08163.x 1:CAS:528:DC%2BC3MXptlSisbs%3D
    • Gatti-Lafranconi P, Natalello A, Ami D, Doglia SM, Lotti M (2011) Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology. FEBS J 278(14):2408-2418. doi: 10.1111/j.1742-4658.2011.08163.x
    • (2011) FEBS J , vol.278 , Issue.14 , pp. 2408-2418
    • Gatti-Lafranconi, P.1    Natalello, A.2    Ami, D.3    Doglia, S.M.4    Lotti, M.5
  • 14
    • 0038463475 scopus 로고    scopus 로고
    • Effects of codon usage versus putative 5-mRNA structure on the expression of Fusarium solani cutinase in the Escherichia coli cytoplasm
    • 10.1016/S1046-5928(02)00578-8 1:CAS:528:DC%2BD38XpvVWlurc%3D
    • Griswold KE, Mahmood NA, Iverson BL, Georgiou G (2003) Effects of codon usage versus putative 5-mRNA structure on the expression of Fusarium solani cutinase in the Escherichia coli cytoplasm. Protein Expres Purif 27(1):134-142
    • (2003) Protein Expres Purif , vol.27 , Issue.1 , pp. 134-142
    • Griswold, K.E.1    Mahmood, N.A.2    Iverson, B.L.3    Georgiou, G.4
  • 15
    • 58749091073 scopus 로고    scopus 로고
    • Chaperone over-expression in Escherichia coli: Apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates
    • 10.1016/j.pep.2008.10.022 1:CAS:528:DC%2BD1MXhtlOltr4%3D
    • Haacke A, Fendrich G, Ramage P, Geiser M (2009) Chaperone over-expression in Escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates. Protein Expres Purif 64(2):185-193
    • (2009) Protein Expres Purif , vol.64 , Issue.2 , pp. 185-193
    • Haacke, A.1    Fendrich, G.2    Ramage, P.3    Geiser, M.4
  • 16
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • 10.1016/S0167-7799(97)01155-4 1:CAS:528:DyaK1cXht1SgtL8%3D
    • Hannig G, Makrides SC (1998) Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol 16(2):54-60
    • (1998) Trends Biotechnol , vol.16 , Issue.2 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 17
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • 10.1038/381571a0 1:CAS:528:DyaK28XjsFyltb8%3D
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381(6583):571-580
    • (1996) Nature , vol.381 , Issue.6583 , pp. 571-580
    • Hartl, F.U.1
  • 18
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • 10.1016/S0021-9673(00)93969-4 1:CAS:528:DyaL1cXhtV2jsrs%3D
    • Hochuli E, Döbeli H, Schacher A (1987) New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J Chromatogr A 411:177-184
    • (1987) J Chromatogr A , vol.411 , pp. 177-184
    • Hochuli, E.1    Döbeli, H.2    Schacher, A.3
  • 19
    • 72049125346 scopus 로고    scopus 로고
    • The N-terminal His-tag and the recombination process affect the biochemical properties of Staphylococcus aureus lipase produced in Escherichia coli
    • 10.1016/j.molcatb.2009.07.002 1:CAS:528:DC%2BD1MXhtlGitrrN
    • Horchani H, Ouertani S, Gargouri Y, Sayari A (2009) The N-terminal His-tag and the recombination process affect the biochemical properties of Staphylococcus aureus lipase produced in Escherichia coli. J Mol Catal B-Enzym 61(3-4):194-201
    • (2009) J Mol Catal B-Enzym , vol.61 , Issue.3-4 , pp. 194-201
    • Horchani, H.1    Ouertani, S.2    Gargouri, Y.3    Sayari, A.4
  • 20
    • 0027318818 scopus 로고
    • Use of repetitive sequences and the polymerase chain reaction technique to classify genetically related Bradyrhizobium japonicum serocluster 123 strains
    • 1:CAS:528:DyaK3sXkvVOnurc%3D
    • Judd AK, Schneider M, Sadowsky MJ, de Bruijn FJ (1993) Use of repetitive sequences and the polymerase chain reaction technique to classify genetically related Bradyrhizobium japonicum serocluster 123 strains. Appl Environ Microb 59(6):1702-1708
    • (1993) Appl Environ Microb , vol.59 , Issue.6 , pp. 1702-1708
    • Judd, A.K.1    Schneider, M.2    Sadowsky, M.J.3    De Bruijn, F.J.4
  • 22
    • 33845756367 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas fluorescens DSM 50106 in E. coli
    • 10.1007/s00253-006-0556-6 10.1007/s00253-006-0556-6 1:CAS:528: DC%2BD28XhtlaqsLrJ
    • Kirschner A, Altenbuchner J, Bornscheuer U (2007) Cloning, expression, and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas fluorescens DSM 50106 in E. coli. Appl Microbiol Biot 73(5):1065-1072. doi: 10.1007/s00253-006-0556-6
    • (2007) Appl Microbiol Biot , vol.73 , Issue.5 , pp. 1065-1072
    • Kirschner, A.1    Altenbuchner, J.2    Bornscheuer, U.3
  • 23
    • 73149103477 scopus 로고    scopus 로고
    • Recombinant Glutamine Synthetase (GS) from C. glutamicum Existed as Both Hexamers & Dedocamers and C-terminal His-tag Enhanced Inclusion Bodies Formation in E. coli
    • 10.1007/s12010-008-8493-8 1:CAS:528:DC%2BD1MXhsVKit7nO
    • Li Y, Yang G, Huang X, Ye B, Liu M, Lin Z, Li C, Cao Z-a (2009) Recombinant Glutamine Synthetase (GS) from C. glutamicum Existed as Both Hexamers & Dedocamers and C-terminal His-tag Enhanced Inclusion Bodies Formation in E. coli. Appl Microbiol Biot 159(3):614-622. doi: 10.1007/s12010-008-8493-8
    • (2009) Appl Microbiol Biot , vol.159 , Issue.3 , pp. 614-622
    • Li, Y.1    Yang, G.2    Huang, X.3    Ye, B.4    Liu, M.5    Lin, Z.6    Li, C.7    Cao, Z.-A.8
  • 24
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli. Curr Opin
    • 1:CAS:528:DyaK1cXntVSgtrk%3D
    • Lilie H, Schwarz E, Rudolph R (1998) Advances in refolding of proteins produced in E. coli. Curr Opin. Biotech 9(5):497-501
    • (1998) Biotech , vol.9 , Issue.5 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 25
    • 1242284596 scopus 로고    scopus 로고
    • An engineered pathway for the formation of protein disulfide bonds
    • 10.1126/science.1092612 10.1126/science.1092612 1:CAS:528: DC%2BD2cXhsVWgtbo%3D
    • Masip L, Pan JL, Haldar S, Penner-Hahn JE, DeLisa MP, Georgiou G, Bardwell JCA, Collet J-F (2004) An engineered pathway for the formation of protein disulfide bonds. Science 303(5661):1185-1189. doi: 10.1126/science. 1092612
    • (2004) Science , vol.303 , Issue.5661 , pp. 1185-1189
    • Masip, L.1    Pan, J.L.2    Haldar, S.3    Penner-Hahn, J.E.4    Delisa, M.P.5    Georgiou, G.6    Bardwell, J.C.A.7    Collet, J.-F.8
  • 26
    • 71649107994 scopus 로고    scopus 로고
    • Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition
    • 10.1016/j.bbapap.2009.10.001 1:CAS:528:DC%2BD1MXhsVGru7vJ
    • Ohtaki A, Murata K, Sato Y, Noguchi K, Miyatake H, Dohmae N, Yamada K, Yohda M, Odaka M (2010) Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition. BBA-Proteins Proteom 1804(1):184-192
    • (2010) BBA-Proteins Proteom , vol.1804 , Issue.1 , pp. 184-192
    • Ohtaki, A.1    Murata, K.2    Sato, Y.3    Noguchi, K.4    Miyatake, H.5    Dohmae, N.6    Yamada, K.7    Yohda, M.8    Odaka, M.9
  • 27
    • 84862805726 scopus 로고    scopus 로고
    • Optimization of purification and refolding of the human chemokine receptor CXCR1 improves the stability of proteoliposomes for structure determination
    • 10.1016/j.bbamem.2011.10.008
    • Park SH, Casagrande F, Chu M, Maier K, Kiefer H, Opella SJ (2011) Optimization of purification and refolding of the human chemokine receptor CXCR1 improves the stability of proteoliposomes for structure determination. BBA-Biomembranes 1818(3):584-591
    • (2011) BBA-Biomembranes , vol.1818 , Issue.3 , pp. 584-591
    • Park, S.H.1    Casagrande, F.2    Chu, M.3    Maier, K.4    Kiefer, H.5    Opella, S.J.6
  • 28
    • 69149097372 scopus 로고    scopus 로고
    • Gene cloning, expression, and characterization of the Geobacillus thermoleovorans CCR11 thermoalkaliphilic lipase
    • 10.1007/s12033-008-9136-6 10.1007/s12033-008-9136-6 1:CAS:528: DC%2BD1MXksVOrt7c%3D
    • Quintana-Castro R, Díaz P, Valerio-Alfaro G, García H, Oliart-Ros R (2009) Gene cloning, expression, and characterization of the Geobacillus thermoleovorans CCR11 thermoalkaliphilic lipase. Mol Biotechnol 42(1):75-83. doi: 10.1007/s12033-008-9136-6
    • (2009) Mol Biotechnol , vol.42 , Issue.1 , pp. 75-83
    • Quintana-Castro, R.1    Díaz, P.2    Valerio-Alfaro, G.3    García, H.4    Oliart-Ros, R.5
  • 29
    • 0028871814 scopus 로고
    • Evaluation of comparative protein modeling by MODELLER
    • 10.1002/prot.340230306 10.1002/prot.340230306
    • Šali A, Potterton L, Yuan F, van Vlijmen H, Karplus M (1995) Evaluation of comparative protein modeling by MODELLER. Proteins 23(3):318-326. doi: 10.1002/prot.340230306
    • (1995) Proteins , vol.23 , Issue.3 , pp. 318-326
    • Šali, A.1    Potterton, L.2    Yuan, F.3    Van Vlijmen, H.4    Karplus, M.5
  • 30
    • 20444433964 scopus 로고    scopus 로고
    • Integrated bioprocesses
    • 10.1016/j.mib.2005.01.002
    • Schügerl K, Hubbuch J (2005) Integrated bioprocesses. Curr Opin Microbiol 8(3):294-300
    • (2005) Curr Opin Microbiol , vol.8 , Issue.3 , pp. 294-300
    • Schügerl, K.1    Hubbuch, J.2
  • 31
    • 79952623795 scopus 로고    scopus 로고
    • Effects of co-expression of molecular chaperones on heterologous soluble expression of the cold-active lipase Lip-948
    • 10.1016/j.pep.2011.01.009
    • Shuo-shuo C, Xue-zheng L, Ji-hong S (2011) Effects of co-expression of molecular chaperones on heterologous soluble expression of the cold-active lipase Lip-948. Protein Expres Purif 77(2):166-172
    • (2011) Protein Expres Purif , vol.77 , Issue.2 , pp. 166-172
    • Shuo-Shuo, C.1    Xue-Zheng, L.2    Ji-Hong, S.3
  • 32
    • 80053640730 scopus 로고    scopus 로고
    • Solubilization of inclusion body proteins using n-propanol and its refolding into bioactive form
    • Singh SM, Sharma A, Upadhyay AK, Singh A, Garg LC, Panda AK (2011) Solubilization of inclusion body proteins using n-propanol and its refolding into bioactive form. Protein Expres Purif 81(1):75-82
    • (2011) Protein Expres Purif , vol.81 , Issue.1 , pp. 75-82
    • Singh, S.M.1    Sharma, A.2    Upadhyay, A.K.3    Singh, A.4    Garg, L.C.5    Panda, A.K.6
  • 33
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • 10.1263/jbb.99.303 1:CAS:528:DC%2BD2MXlsFCnsrc%3D
    • Singh SM, Panda AK (2005) Solubilization and refolding of bacterial inclusion body proteins. J Biosci Bioeng 99(4):303-310
    • (2005) J Biosci Bioeng , vol.99 , Issue.4 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 34
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • 10.1016/j.jbiotec.2004.08.004
    • Sørensen HP, Mortensen KK (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol 115(2):113-128
    • (2005) J Biotechnol , vol.115 , Issue.2 , pp. 113-128
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 35
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • 10.1007/s00253-002-1158-6 1:CAS:528:DC%2BD3sXjvFGntQ%3D%3D
    • Terpe K (2003) Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biot 60(5):523-533. doi: 10.1007/s00253-002-1158-6
    • (2003) Appl Microbiol Biot , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 36
    • 33747666218 scopus 로고    scopus 로고
    • Overview of bacterial expression systems for heterologous protein production: From molecular and biochemical fundamentals to commercial systems
    • 10.1007/s00253-006-0465-8 10.1007/s00253-006-0465-8 1:CAS:528: DC%2BD28XotlCiu7k%3D
    • Terpe K (2006) Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biot 72(2):211-222. doi: 10.1007/s00253-006-0465-8
    • (2006) Appl Microbiol Biot , vol.72 , Issue.2 , pp. 211-222
    • Terpe, K.1
  • 37
    • 0345636051 scopus 로고    scopus 로고
    • Practical considerations in refolding proteins from inclusion bodies
    • 10.1016/S1046-5928(02)00641-1 1:CAS:528:DC%2BD3sXitVKnu7Y%3D
    • Tsumoto K, Ejima D, Kumagai I, Arakawa T (2003) Practical considerations in refolding proteins from inclusion bodies. Protein Expres Purif 28(1):1-8
    • (2003) Protein Expres Purif , vol.28 , Issue.1 , pp. 1-8
    • Tsumoto, K.1    Ejima, D.2    Kumagai, I.3    Arakawa, T.4
  • 38
    • 57249095871 scopus 로고    scopus 로고
    • Functional expression of porcine aminoacylase 1 in E. coli using a codon optimized synthetic gene and molecular chaperones
    • 10.1007/s00253-008-1716-7 10.1007/s00253-008-1716-7 1:CAS:528: DC%2BD1cXhsVCntb3O
    • Wardenga R, Hollmann F, Thum O, Bornscheuer U (2008) Functional expression of porcine aminoacylase 1 in E. coli using a codon optimized synthetic gene and molecular chaperones. Appl Microbiol Biot 81(4):721-729. doi: 10.1007/s00253-008-1716-7
    • (2008) Appl Microbiol Biot , vol.81 , Issue.4 , pp. 721-729
    • Wardenga, R.1    Hollmann, F.2    Thum, O.3    Bornscheuer, U.4


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