메뉴 건너뛰기




Volumn 16, Issue 2, 2015, Pages 67-80

Expression platforms for producing eukaryotic proteins: a comparison of E. coli cell-based and wheat germ cell-free synthesis, affinity and solubility tags, and cloning strategies

Author keywords

Flexi Vector cloning; Gateway cloning; Maltose Binding Protein solubility tag; NIH Protein Structure Initiative; Structural genomics; Wheat germ cell free translation

Indexed keywords

PROTEIN;

EID: 84937761852     PISSN: 1345711X     EISSN: 15700267     Source Type: Journal    
DOI: 10.1007/s10969-015-9198-1     Document Type: Article
Times cited : (10)

References (42)
  • 2
  • 4
    • 0036362061 scopus 로고    scopus 로고
    • Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins
    • COI: 1:CAS:528:DC%2BD38XosValsLY%3D, PID: 12836665
    • Routzahn KM, Waugh DS (2002) Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins. J Struct Funct Genomics 2(2):83–92
    • (2002) J Struct Funct Genomics , vol.2 , Issue.2 , pp. 83-92
    • Routzahn, K.M.1    Waugh, D.S.2
  • 6
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • COI: 1:CAS:528:DC%2BD38XosFyluw%3D%3D, PID: 11790841
    • Hammarstrom M, Hellgren N, van Den Berg S, Berglund H, Hard T (2002) Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci 11(2):313–321
    • (2002) Protein Sci , vol.11 , Issue.2 , pp. 313-321
    • Hammarstrom, M.1    Hellgren, N.2    van Den Berg, S.3    Berglund, H.4    Hard, T.5
  • 8
    • 0028329918 scopus 로고
    • Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase
    • COI: 1:CAS:528:DyaK2cXhsFOktLg%3D, PID: 8179197
    • Parks TD, Leuther KK, Howard ED, Johnston SA, Dougherty WG (1994) Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase. Anal Biochem 216(2):413–417
    • (1994) Anal Biochem , vol.216 , Issue.2 , pp. 413-417
    • Parks, T.D.1    Leuther, K.K.2    Howard, E.D.3    Johnston, S.A.4    Dougherty, W.G.5
  • 9
    • 0141558969 scopus 로고    scopus 로고
    • Construction of an efficient expression vector for coupled transcription/translation in a wheat germ cell-free system
    • PID: 12903243
    • Sawasaki T, Hasegawa Y, Tsuchimochi M, Kasahara Y, Endo Y (2000) Construction of an efficient expression vector for coupled transcription/translation in a wheat germ cell-free system. Nucleic Acids Symp Ser 44:9–10
    • (2000) Nucleic Acids Symp Ser , vol.44 , pp. 9-10
    • Sawasaki, T.1    Hasegawa, Y.2    Tsuchimochi, M.3    Kasahara, Y.4    Endo, Y.5
  • 10
    • 14344255383 scopus 로고    scopus 로고
    • High-throughput automated platform for nuclear magnetic resonance-based structural proteomics
    • COI: 1:CAS:528:DC%2BD2MXis1Knt70%3D, PID: 15966852
    • Vinarov DA, Markley JL (2005) High-throughput automated platform for nuclear magnetic resonance-based structural proteomics. Expert Rev Proteomics 2(1):49–55
    • (2005) Expert Rev Proteomics , vol.2 , Issue.1 , pp. 49-55
    • Vinarov, D.A.1    Markley, J.L.2
  • 12
    • 33646572265 scopus 로고    scopus 로고
    • High efficiency single step production of expression plasmids from cDNA clones using the Flexi Vector cloning system
    • COI: 1:CAS:528:DC%2BD28XltVKitLY%3D, PID: 16377204
    • Blommel PG, Martin PA, Wrobel RL, Steffen E, Fox BG (2006) High efficiency single step production of expression plasmids from cDNA clones using the Flexi Vector cloning system. Protein Expr Purif 47(2):562–570
    • (2006) Protein Expr Purif , vol.47 , Issue.2 , pp. 562-570
    • Blommel, P.G.1    Martin, P.A.2    Wrobel, R.L.3    Steffen, E.4    Fox, B.G.5
  • 13
    • 0033732564 scopus 로고    scopus 로고
    • GATEWAY recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes
    • COI: 1:CAS:528:DC%2BD3cXosFSjtrc%3D, PID: 11075367
    • Walhout AJ, Temple GF, Brasch MA, Hartley JL, Lorson MA, van den Heuvel S, Vidal M (2000) GATEWAY recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes. Methods Enzymol 328:575–592
    • (2000) Methods Enzymol , vol.328 , pp. 575-592
    • Walhout, A.J.1    Temple, G.F.2    Brasch, M.A.3    Hartley, J.L.4    Lorson, M.A.5    van den Heuvel, S.6    Vidal, M.7
  • 15
    • 14344256801 scopus 로고    scopus 로고
    • Cell-free protein production and labeling protocol for NMR-based structural proteomics
    • COI: 1:CAS:528:DC%2BD2MXisVGhu7g%3D, PID: 15782178
    • Vinarov DA, Lytle BL, Peterson FC, Tyler EM, Volkman BF, Markley JL (2004) Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat Methods 1(2):149–153
    • (2004) Nat Methods , vol.1 , Issue.2 , pp. 149-153
    • Vinarov, D.A.1    Lytle, B.L.2    Peterson, F.C.3    Tyler, E.M.4    Volkman, B.F.5    Markley, J.L.6
  • 17
    • 77952755494 scopus 로고    scopus 로고
    • Cell-free protein synthesis technology in NMR high-throughput structure determination
    • COI: 1:CAS:528:DC%2BC3cXosl2jsL0%3D, PID: 20204854
    • Makino S, Goren MA, Fox BG, Markley JL (2010) Cell-free protein synthesis technology in NMR high-throughput structure determination. Methods Mol Biol 607:127–147
    • (2010) Methods Mol Biol , vol.607 , pp. 127-147
    • Makino, S.1    Goren, M.A.2    Fox, B.G.3    Markley, J.L.4
  • 21
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • COI: 1:CAS:528:DyaK2MXhtVSmurfK, PID: 8520220
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 23
    • 34250316620 scopus 로고    scopus 로고
    • Enhanced bacterial protein expression during auto-induction obtained by alteration of lac repressor dosage and medium composition
    • COI: 1:CAS:528:DC%2BD2sXlt1ylt7s%3D, PID: 17506520
    • Blommel PG, Becker KJ, Duvnjak P, Fox BG (2007) Enhanced bacterial protein expression during auto-induction obtained by alteration of lac repressor dosage and medium composition. Biotechnol Prog 23(3):585–598
    • (2007) Biotechnol Prog , vol.23 , Issue.3 , pp. 585-598
    • Blommel, P.G.1    Becker, K.J.2    Duvnjak, P.3    Fox, B.G.4
  • 24
    • 77951220185 scopus 로고    scopus 로고
    • Crystal structure of an eIF4G-like protein from Danio rerio
    • COI: 1:CAS:528:DC%2BC3cXks1KgsL0%3D, PID: 20229607
    • Bae E, Bitto E, Bingman CA, McCoy JG, Wesenberg GE, Phillips GN Jr (2010) Crystal structure of an eIF4G-like protein from Danio rerio. Proteins 78(7):1803–1806
    • (2010) Proteins , vol.78 , Issue.7 , pp. 1803-1806
    • Bae, E.1    Bitto, E.2    Bingman, C.A.3    McCoy, J.G.4    Wesenberg, G.E.5    Phillips, G.N.6
  • 25
    • 37349082442 scopus 로고    scopus 로고
    • Structure and dynamics of gamma-SNAP: insight into flexibility of proteins from the SNAP family
    • COI: 1:CAS:528:DC%2BD1cXisVamuw%3D%3D, PID: 17634982
    • Bitto E, Bingman CA, Kondrashov DA, McCoy JG, Bannen RM, Wesenberg GE, Phillips GN Jr (2008) Structure and dynamics of gamma-SNAP: insight into flexibility of proteins from the SNAP family. Proteins 70(1):93–104
    • (2008) Proteins , vol.70 , Issue.1 , pp. 93-104
    • Bitto, E.1    Bingman, C.A.2    Kondrashov, D.A.3    McCoy, J.G.4    Bannen, R.M.5    Wesenberg, G.E.6    Phillips, G.N.7
  • 26
    • 0035983443 scopus 로고    scopus 로고
    • The P1′ specificity of tobacco etch virus protease
    • COI: 1:CAS:528:DC%2BD38Xks1Gnt7s%3D, PID: 12074568
    • Kapust RB, Tozser J, Copeland TD, Waugh DS (2002) The P1′ specificity of tobacco etch virus protease. Biochem Biophys Res Commun 294(5):949–955
    • (2002) Biochem Biophys Res Commun , vol.294 , Issue.5 , pp. 949-955
    • Kapust, R.B.1    Tozser, J.2    Copeland, T.D.3    Waugh, D.S.4
  • 28
    • 0032006484 scopus 로고    scopus 로고
    • Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin
    • COI: 1:CAS:528:DyaK1cXht1yhsbY%3D, PID: 9473466
    • Sachdev D, Chirgwin JM (1998) Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin. Protein Expr Purif 12(1):122–132
    • (1998) Protein Expr Purif , vol.12 , Issue.1 , pp. 122-132
    • Sachdev, D.1    Chirgwin, J.M.2
  • 29
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • COI: 1:CAS:528:DyaK1MXlt1Omu7g%3D, PID: 10452611
    • Kapust RB, Waugh DS (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8(8):1668–1674
    • (1999) Protein Sci , vol.8 , Issue.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 30
    • 33644774471 scopus 로고    scopus 로고
    • Optimal isotope labelling for NMR protein structure determinations
    • COI: 1:CAS:528:DC%2BD28XhvFajtL4%3D, PID: 16511487
    • Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Guntert P (2006) Optimal isotope labelling for NMR protein structure determinations. Nature 440(7080):52–57
    • (2006) Nature , vol.440 , Issue.7080 , pp. 52-57
    • Kainosho, M.1    Torizawa, T.2    Iwashita, Y.3    Terauchi, T.4    Mei Ono, A.5    Guntert, P.6
  • 31
    • 33750489405 scopus 로고    scopus 로고
    • Incorporating a TEV cleavage site reduces the solubility of nine recombinant mouse proteins
    • COI: 1:CAS:528:DC%2BD28XhtFKmt7rO, PID: 16798010
    • Kurz M, Cowieson NP, Robin G, Hume DA, Martin JL, Kobe B, Listwan P (2006) Incorporating a TEV cleavage site reduces the solubility of nine recombinant mouse proteins. Protein Expr Purif 50(1):68–73
    • (2006) Protein Expr Purif , vol.50 , Issue.1 , pp. 68-73
    • Kurz, M.1    Cowieson, N.P.2    Robin, G.3    Hume, D.A.4    Martin, J.L.5    Kobe, B.6    Listwan, P.7
  • 33
    • 0024431580 scopus 로고
    • Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli
    • COI: 1:CAS:528:DyaK3cXjtFKhtA%3D%3D, PID: 2555540
    • Cordingley MG, Register RB, Callahan PL, Garsky VM, Colonno RJ (1989) Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli. J Virol 63(12):5037–5045
    • (1989) J Virol , vol.63 , Issue.12 , pp. 5037-5045
    • Cordingley, M.G.1    Register, R.B.2    Callahan, P.L.3    Garsky, V.M.4    Colonno, R.J.5
  • 35
    • 34250348569 scopus 로고    scopus 로고
    • A combined approach to improving large-scale production of tobacco etch virus protease
    • COI: 1:CAS:528:DC%2BD2sXpt1amsr0%3D, PID: 17543538
    • Blommel PG, Fox BG (2007) A combined approach to improving large-scale production of tobacco etch virus protease. Protein Expr Purif 55(1):53–68
    • (2007) Protein Expr Purif , vol.55 , Issue.1 , pp. 53-68
    • Blommel, P.G.1    Fox, B.G.2
  • 36
    • 80054052318 scopus 로고    scopus 로고
    • An overview of enzymatic reagents for the removal of affinity tags
    • COI: 1:CAS:528:DC%2BC3MXhtlejtLvL, PID: 21871965
    • Waugh DS (2011) An overview of enzymatic reagents for the removal of affinity tags. Protein Expr Purif 80(2):283–293
    • (2011) Protein Expr Purif , vol.80 , Issue.2 , pp. 283-293
    • Waugh, D.S.1
  • 37
    • 59249094982 scopus 로고    scopus 로고
    • SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems
    • COI: 1:CAS:528:DC%2BD1cXhsVait7bP, PID: 19107426
    • Panavas T, Sanders C, Butt TR (2009) SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems. Methods Mol Biol 497:303–317
    • (2009) Methods Mol Biol , vol.497 , pp. 303-317
    • Panavas, T.1    Sanders, C.2    Butt, T.R.3
  • 38
    • 8744294716 scopus 로고    scopus 로고
    • Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification
    • COI: 1:CAS:528:DC%2BD2cXovFKrsLw%3D, PID: 15544324
    • Ruan B, Fisher KE, Alexander PA, Doroshko V, Bryan PN (2004) Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification. Biochemistry 43(46):14539–14546
    • (2004) Biochemistry , vol.43 , Issue.46 , pp. 14539-14546
    • Ruan, B.1    Fisher, K.E.2    Alexander, P.A.3    Doroshko, V.4    Bryan, P.N.5
  • 39
    • 33748289981 scopus 로고    scopus 로고
    • Wheat germ cell-free platform for eukaryotic protein production
    • COI: 1:CAS:528:DC%2BD28Xht1yqsrrI, PID: 16930128
    • Vinarov DA, Loushin Newman CL, Markley JL (2006) Wheat germ cell-free platform for eukaryotic protein production. FEBS J 273(18):4160–4169
    • (2006) FEBS J , vol.273 , Issue.18 , pp. 4160-4169
    • Vinarov, D.A.1    Loushin Newman, C.L.2    Markley, J.L.3
  • 40
    • 84872742965 scopus 로고    scopus 로고
    • Function of Shaker potassium channels produced by cell-free translation upon injection into Xenopus oocytes
    • PID: 23301161
    • Jarecki BW, Makino S, Beebe ET, Fox BG, Chanda B (2013) Function of Shaker potassium channels produced by cell-free translation upon injection into Xenopus oocytes. Sci Rep 3:1040
    • (2013) Sci Rep , vol.3 , pp. 1040
    • Jarecki, B.W.1    Makino, S.2    Beebe, E.T.3    Fox, B.G.4    Chanda, B.5
  • 42
    • 84888112788 scopus 로고    scopus 로고
    • Cell-free production of integral membrane aspartic acid proteases reveals zinc-dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD
    • Aly KA, Beebe ET, Chan CH, Goren MA, Sepúlveda C, Makino SI, Fox BG, Forest KT (2013) Cell-free production of integral membrane aspartic acid proteases reveals zinc-dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD. Microbiol Open 2(1):94–104
    • (2013) Microbiol Open , vol.2 , Issue.1 , pp. 94-104
    • Aly, K.A.1    Beebe, E.T.2    Chan, C.H.3    Goren, M.A.4    Sepúlveda, C.5    Makino, S.I.6    Fox, B.G.7    Forest, K.T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.