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Volumn 5, Issue FEB, 2014, Pages

Generation of a vector suite for protein solubility screening

Author keywords

Cloning; Expression; High throughput; Recombinant proteins; Solubility; Vector

Indexed keywords

GLUCAN SYNTHASE; GREEN FLUORESCENT PROTEIN; MALTOSE BINDING PROTEIN; POLYHISTIDINE TAG; PROTEIN DISULFIDE ISOMERASE; RECOMBINANT PROTEIN; SUMO 2 PROTEIN; THIOREDOXIN;

EID: 84897630667     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00067     Document Type: Article
Times cited : (24)

References (35)
  • 1
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • doi: 10.1093/nar/18.20.6069
    • Aslanidis, C., and de Jong, P. J. (1990). Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18, 6069-6074. doi: 10.1093/nar/18.20.6069
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 2
    • 34247846396 scopus 로고    scopus 로고
    • A versatile ligation-independent cloning method suitable for high-throughput expression screening applications
    • doi: 10.1093/nar/gkm047
    • Berrow, N. S., Alderton, D., Sainsbury, S., Nettleship, J., Assenberg, R., Rahman, N., et al. (2007). A versatile ligation-independent cloning method suitable for high-throughput expression screening applications. Nucleic Acids Res. 35, e45. doi: 10.1093/nar/gkm047
    • (2007) Nucleic Acids Res. , vol.35
    • Berrow, N.S.1    Alderton, D.2    Sainsbury, S.3    Nettleship, J.4    Assenberg, R.5    Rahman, N.6
  • 3
    • 33645471986 scopus 로고    scopus 로고
    • A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production
    • doi: 10.1186/1472-6750-6-12
    • Cabrita, L. D., Dai, W., and Bottomley, S. P. (2006). A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production. BMC Biotechnol. 6:12. doi: 10.1186/1472-6750-6-12
    • (2006) BMC Biotechnol. , vol.6 , pp. 12
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 4
    • 0026557995 scopus 로고
    • Inclusion bodies of the thermophilic endoglucanase D from Clostridium thermocellum are made of native enzyme that resists 8 M urea
    • doi: 10.1111/j.1432-1033.1992.tb16789.x
    • Chaffotte, A. F., Guillou, Y., and Goldberg, M. E. (1992). Inclusion bodies of the thermophilic endoglucanase D from Clostridium thermocellum are made of native enzyme that resists 8 M urea. Eur. J. Biochem. 205, 369-373. doi: 10.1111/j.1432-1033.1992.tb16789.x
    • (1992) Eur. J. Biochem. , vol.205 , pp. 369-373
    • Chaffotte, A.F.1    Guillou, Y.2    Goldberg, M.E.3
  • 5
    • 32644478232 scopus 로고    scopus 로고
    • Enhanced soluble protein expression using two new fusion tags
    • doi: 10.1016/j.pep.2005.07.028
    • Chatterjee, D. K., and Esposito, D. (2006). Enhanced soluble protein expression using two new fusion tags. Protein Expr. Purif. 46, 122-129. doi: 10.1016/j.pep.2005.07.028
    • (2006) Protein Expr. Purif. , vol.46 , pp. 122-129
    • Chatterjee, D.K.1    Esposito, D.2
  • 6
    • 78149464373 scopus 로고    scopus 로고
    • EspA is a novel fusion partner for expression of foreign proteins in Escherichia coli
    • doi: 10.1016/j.jbiotec.2010.09.940
    • Cheng, Y., Gu, J., Wang, H. G., Yu, S., Liu, Y. Q., Ning, Y. L., et al. (2010). EspA is a novel fusion partner for expression of foreign proteins in Escherichia coli. J. Biotechnol. 150, 380-388. doi: 10.1016/j.jbiotec.2010.09.940
    • (2010) J. Biotechnol. , vol.150 , pp. 380-388
    • Cheng, Y.1    Gu, J.2    Wang, H.G.3    Yu, S.4    Liu, Y.Q.5    Ning, Y.L.6
  • 7
    • 79957875229 scopus 로고    scopus 로고
    • Tuning different expression parameters to achieve soluble recombinant proteins in E. coli: advantages of high-throughput screening
    • doi: 10.1002/biot.201100025
    • Correa, A., and Oppezzo, P. (2011). Tuning different expression parameters to achieve soluble recombinant proteins in E. coli: advantages of high-throughput screening. Biotechnol. J. 6, 715-730. doi: 10.1002/biot.201100025
    • (2011) Biotechnol. J. , vol.6 , pp. 715-730
    • Correa, A.1    Oppezzo, P.2
  • 8
    • 78650175862 scopus 로고    scopus 로고
    • The pURI family of expression vectors: a versatile set of ligation independent cloning plasmids for producing recombinant His-fusion proteins
    • doi: 10.1016/j.pep.2010.10.013
    • Curiel, J. A., De Las Rivas, B., Mancheno, J. M., and Munoz, R. (2010). The pURI family of expression vectors: a versatile set of ligation independent cloning plasmids for producing recombinant His-fusion proteins. Protein Expr. Purif. 76, 44-53. doi: 10.1016/j.pep.2010.10.013
    • (2010) Protein Expr. Purif. , vol.76 , pp. 44-53
    • Curiel, J.A.1    De Las Rivas, B.2    Mancheno, J.M.3    Munoz, R.4
  • 9
    • 34250665073 scopus 로고    scopus 로고
    • Colony filtration blotting for screening soluble expression in Escherichia coli
    • doi: 10.1038/nprot.2006.39
    • Dahlroth, S. L., Nordlund, P., and Cornvik, T. (2006). Colony filtration blotting for screening soluble expression in Escherichia coli. Nat. Protoc. 1, 253-258. doi: 10.1038/nprot.2006.39
    • (2006) Nat. Protoc. , vol.1 , pp. 253-258
    • Dahlroth, S.L.1    Nordlund, P.2    Cornvik, T.3
  • 10
    • 84954358425 scopus 로고    scopus 로고
    • Mocr: a novel fusion tag for enhancing solubility that is compatible with structural biology applications
    • doi: 10.1016/j.pep.2008.08.011
    • DelProposto, J., Majmudar, C. Y., Smith, J. L., and Brown, W. C. (2009). Mocr: a novel fusion tag for enhancing solubility that is compatible with structural biology applications. Protein Expr. Purif. 63, 40-49. doi: 10.1016/j.pep.2008.08.011
    • (2009) Protein Expr. Purif. , vol.63 , pp. 40-49
    • DelProposto, J.1    Majmudar, C.Y.2    Smith, J.L.3    Brown, W.C.4
  • 11
    • 84934442053 scopus 로고    scopus 로고
    • Gateway cloning for protein expression
    • doi: 10.1007/978-1-59745-196-3_3
    • Esposito, D., Garvey, L. A., and Chakiath, C. S. (2009). Gateway cloning for protein expression. Methods Mol. Biol. 498, 31-54. doi: 10.1007/978-1-59745-196-3_3
    • (2009) Methods Mol. Biol. , vol.498 , pp. 31-54
    • Esposito, D.1    Garvey, L.A.2    Chakiath, C.S.3
  • 12
    • 0035983443 scopus 로고    scopus 로고
    • The P1' specificity of tobacco etch virus protease
    • doi: 10.1016/S0006-291X(02)00574-0
    • Kapust, R. B., Tozser, J., Copeland, T. D., and Waugh, D. S. (2002). The P1' specificity of tobacco etch virus protease. Biochem. Biophys. Res. Commun. 294, 949-955. doi: 10.1016/S0006-291X(02)00574-0
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 949-955
    • Kapust, R.B.1    Tozser, J.2    Copeland, T.D.3    Waugh, D.S.4
  • 13
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • doi: 10.1110/ps.8.8.1668
    • Kapust, R. B., and Waugh, D. S. (1999). Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8, 1668-1674. doi: 10.1110/ps.8.8.1668
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 14
    • 0030821002 scopus 로고    scopus 로고
    • Interaction between Clostridium thermocellum endoglucanase CelD and polypeptides derived from the cellulosome-integrating protein CipA: stoichiometry and cellulolytic activity of the complexes
    • Kataeva, I., Guglielmi, G., and Beguin, P. (1997). Interaction between Clostridium thermocellum endoglucanase CelD and polypeptides derived from the cellulosome-integrating protein CipA: stoichiometry and cellulolytic activity of the complexes. Biochem. J. 326 (Pt 2), 617-624.
    • (1997) Biochem. J. , vol.326 , Issue.PART 2 , pp. 617-624
    • Kataeva, I.1    Guglielmi, G.2    Beguin, P.3
  • 15
    • 0011962568 scopus 로고    scopus 로고
    • Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli
    • doi: 10.1016/S0076-6879(00)26063-1
    • LaVallie, E. R., Lu, Z., Diblasio-Smith, E. A., Collins-Racie, L. A., and McCoy, J. M. (2000). Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli. Methods Enzymol. 326, 322-340. doi: 10.1016/S0076-6879(00)26063-1
    • (2000) Methods Enzymol. , vol.326 , pp. 322-340
    • LaVallie, E.R.1    Lu, Z.2    Diblasio-Smith, E.A.3    Collins-Racie, L.A.4    McCoy, J.M.5
  • 16
    • 79959549028 scopus 로고    scopus 로고
    • Enabling high-throughput ligation-independent cloning and protein expression for the family of ubiquitin specific proteases
    • doi: 10.1016/j.jsb.2011.03.017
    • Luna-Vargas, M. P., Christodoulou, E., Alfieri, A., Van Dijk, W. J., Stadnik, M., Hibbert, R. G., et al. (2011). Enabling high-throughput ligation-independent cloning and protein expression for the family of ubiquitin specific proteases. J. Struct. Biol. 175, 113-119. doi: 10.1016/j.jsb.2011.03.017
    • (2011) J. Struct. Biol. , vol.175 , pp. 113-119
    • Luna-Vargas, M.P.1    Christodoulou, E.2    Alfieri, A.3    Van Dijk, W.J.4    Stadnik, M.5    Hibbert, R.G.6
  • 17
  • 18
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO
    • doi: 10.1110/ps.051812706
    • Marblestone, J. G., Edavettal, S. C., Lim, Y., Lim, P., Zuo, X., and Butt, T. R. (2006). Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO. Protein Sci. 15, 182-189. doi: 10.1110/ps.051812706
    • (2006) Protein Sci. , vol.15 , pp. 182-189
    • Marblestone, J.G.1    Edavettal, S.C.2    Lim, Y.3    Lim, P.4    Zuo, X.5    Butt, T.R.6
  • 19
    • 33644809741 scopus 로고    scopus 로고
    • High-throughput purification of hexahistidine-tagged proteins expressed in E
    • doi: 10.1007/978-1-59259-948-6_9
    • Murphy, M. B., and Doyle, S. A. (2005). High-throughput purification of hexahistidine-tagged proteins expressed in E. coli. Methods Mol. Biol. 310, 123-130. doi: 10.1007/978-1-59259-948-6_9
    • (2005) coli. Methods Mol. Biol. , vol.310 , pp. 123-130
    • Murphy, M.B.1    Doyle, S.A.2
  • 20
    • 84865960733 scopus 로고    scopus 로고
    • Structural basis for benzothiazinone-mediated killing of Mycobacterium tuberculosis
    • doi: 10.1126/scitranslmed.3004395
    • Neres, J., Pojer, F., Molteni, E., Chiarelli, L. R., Dhar, N., Boy-Rottger, S., et al. (2012). Structural basis for benzothiazinone-mediated killing of Mycobacterium tuberculosis. Sci. Transl. Med. 4, 150ra121. doi: 10.1126/scitranslmed.3004395
    • (2012) Sci. Transl. Med. , vol.4 , pp. 121-150
    • Neres, J.1    Pojer, F.2    Molteni, E.3    Chiarelli, L.R.4    Dhar, N.5    Boy-Rottger, S.6
  • 21
    • 84876734643 scopus 로고    scopus 로고
    • High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E
    • doi: 10.1186/1475-2859-12-37
    • Nozach, H., Fruchart-Gaillard, C., Fenaille, F., Beau, F., Ramos, O. H., Douzi, B., et al. (2013). High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli. Microb. Cell Fact. 12, 37. doi: 10.1186/1475-2859-12-37
    • (2013) coli. Microb. Cell Fact. , vol.12 , pp. 37
    • Nozach, H.1    Fruchart-Gaillard, C.2    Fenaille, F.3    Beau, F.4    Ramos, O.H.5    Douzi, B.6
  • 22
    • 84934435566 scopus 로고    scopus 로고
    • High-throughput expression screening and purification of recombinant proteins in E
    • doi: 10.1007/978-1-62703-691-7_3
    • Saez, N. J., and Vincentelli, R. (2013). High-throughput expression screening and purification of recombinant proteins in E. coli. Methods Mol. Biol. 1091, 33-53. doi: 10.1007/978-1-62703-691-7_3
    • (2013) coli. Methods Mol. Biol. , vol.1091 , pp. 33-53
    • Saez, N.J.1    Vincentelli, R.2
  • 23
    • 79957534528 scopus 로고    scopus 로고
    • The ribosome binding site calculator
    • doi: 10.1016/B978-0-12-385120-8.00002-4
    • Salis, H. M. (2011). The ribosome binding site calculator. Methods Enzymol. 498, 19-42. doi: 10.1016/B978-0-12-385120-8.00002-4
    • (2011) Methods Enzymol. , vol.498 , pp. 19-42
    • Salis, H.M.1
  • 24
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • doi: 10.1038/nbt.1568
    • Salis, H. M., Mirsky, E. A., and Voigt, C. A. (2009). Automated design of synthetic ribosome binding sites to control protein expression. Nat. Biotechnol. 27, 946-950. doi: 10.1038/nbt.1568
    • (2009) Nat. Biotechnol. , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 26
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • doi: 10.1038/nprot.2007.209
    • Schmidt, T. G., and Skerra, A. (2007). The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat. Protoc. 2, 1528-1535. doi: 10.1038/nprot.2007.209
    • (2007) Nat. Protoc. , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 27
    • 79959883233 scopus 로고    scopus 로고
    • A novel Escherichia coli solubility enhancer protein for fusion expression of aggregation-prone heterologous proteins
    • doi: 10.1016/j.enzmictec.2011.04.013
    • Song, J. A., Lee, D. S., Park, J. S., Han, K. Y., and Lee, J. (2011). A novel Escherichia coli solubility enhancer protein for fusion expression of aggregation-prone heterologous proteins. Enzyme Microb. Technol. 49, 124-130. doi: 10.1016/j.enzmictec.2011.04.013
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 124-130
    • Song, J.A.1    Lee, D.S.2    Park, J.S.3    Han, K.Y.4    Lee, J.5
  • 28
    • 33645417226 scopus 로고    scopus 로고
    • High-throughput protein purification using an automated set-up for high-yield affinity chromatography
    • doi: 10.1016/j.pep.2005.12.010
    • Steen, J., Uhlen, M., Hober, S., and Ottosson, J. (2006). High-throughput protein purification using an automated set-up for high-yield affinity chromatography. Protein Expr. Purif. 46, 173-178. doi: 10.1016/j.pep.2005.12.010
    • (2006) Protein Expr. Purif. , vol.46 , pp. 173-178
    • Steen, J.1    Uhlen, M.2    Hober, S.3    Ottosson, J.4
  • 29
    • 77956184308 scopus 로고    scopus 로고
    • Applications of the restriction free (RF) cloning procedure for molecular manipulations and protein expression
    • doi: 10.1016/j.jsb.2010.06.016
    • Unger, T., Jacobovitch, Y., Dantes, A., Bernheim, R., and Peleg, Y. (2010). Applications of the restriction free (RF) cloning procedure for molecular manipulations and protein expression. J. Struct. Biol. 172, 34-44. doi: 10.1016/j.jsb.2010.06.016
    • (2010) J. Struct. Biol. , vol.172 , pp. 34-44
    • Unger, T.1    Jacobovitch, Y.2    Dantes, A.3    Bernheim, R.4    Peleg, Y.5
  • 30
    • 30944459888 scopus 로고    scopus 로고
    • Improved solubility of TEV protease by directed evolution
    • doi: 10.1016/j.jbiotec.2005.08.006
    • van den Berg, S., Lofdahl, P. A., Hard, T., and Berglund, H. (2006). Improved solubility of TEV protease by directed evolution. J. Biotechnol. 121, 291-298. doi: 10.1016/j.jbiotec.2005.08.006
    • (2006) J. Biotechnol. , vol.121 , pp. 291-298
    • van den Berg, S.1    Lofdahl, P.A.2    Hard, T.3    Berglund, H.4
  • 31
    • 80053631355 scopus 로고    scopus 로고
    • High-throughput protein expression screening and purification in Escherichia coli
    • doi: 10.1016/j.ymeth.2011.08.010
    • Vincentelli, R., Cimino, A., Geerlof, A., Kubo, A., Satou, Y., and Cambillau, C. (2011). High-throughput protein expression screening and purification in Escherichia coli. Methods 55, 65-72. doi: 10.1016/j.ymeth.2011.08.010
    • (2011) Methods , vol.55 , pp. 65-72
    • Vincentelli, R.1    Cimino, A.2    Geerlof, A.3    Kubo, A.4    Satou, Y.5    Cambillau, C.6
  • 32
    • 84879147807 scopus 로고    scopus 로고
    • Expression in Escherichia coli: becoming faster and more complex
    • doi: 10.1016/j.sbi.2013.01.006
    • Vincentelli, R., and Romier, C. (2013). Expression in Escherichia coli: becoming faster and more complex. Curr. Opin. Struct. Biol. 23, 326-334. doi: 10.1016/j.sbi.2013.01.006
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 326-334
    • Vincentelli, R.1    Romier, C.2
  • 33
    • 0033015460 scopus 로고    scopus 로고
    • Rapid protein-folding assay using green fluorescent protein
    • doi: 10.1038/10904
    • Waldo, G. S., Standish, B. M., Berendzen, J., and Terwilliger, T. C. (1999). Rapid protein-folding assay using green fluorescent protein. Nat. Biotechnol. 17, 691-695. doi: 10.1038/10904
    • (1999) Nat. Biotechnol. , vol.17 , pp. 691-695
    • Waldo, G.S.1    Standish, B.M.2    Berendzen, J.3    Terwilliger, T.C.4
  • 34
    • 84860309632 scopus 로고    scopus 로고
    • Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications
    • doi: 10.1002/biot.201100155
    • Young, C. L., Britton, Z. T., and Robinson, A. S. (2012). Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications. Biotechnol. J. 7, 620-634. doi: 10.1002/biot.201100155
    • (2012) Biotechnol. J. , vol.7 , pp. 620-634
    • Young, C.L.1    Britton, Z.T.2    Robinson, A.S.3
  • 35
    • 77956185960 scopus 로고    scopus 로고
    • ESPRIT: an automated, library-based method for mapping and soluble expression of protein domains from challenging targets
    • doi: 10.1016/j.jsb.2010.02.021
    • Yumerefendi, H., Tarendeau, F., Mas, P. J., and Hart, D. J. (2010). ESPRIT: an automated, library-based method for mapping and soluble expression of protein domains from challenging targets. J. Struct. Biol. 172, 66-74. doi: 10.1016/j.jsb.2010.02.021
    • (2010) J. Struct. Biol. , vol.172 , pp. 66-74
    • Yumerefendi, H.1    Tarendeau, F.2    Mas, P.J.3    Hart, D.J.4


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