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Volumn 4, Issue 6, 2005, Pages 1942-1951

Improving solubility of Shewanella oneidensis MR-1 and Clostridium thermocellum JW-20 proteins expressed into Esherichia coli

Author keywords

Gene cloning and expression; Improvement of protein solubility; Role of fusions on protein solubility

Indexed keywords

AMPICILLIN; BACTERIAL PROTEIN; GENOMIC DNA; JW 20 PROTEIN; MALTOSE BINDING PROTEIN; MR 1 PROTEIN; POLYPEPTIDE; UNCLASSIFIED DRUG;

EID: 29144497227     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr050108j     Document Type: Article
Times cited : (44)

References (47)
  • 1
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx, F.; Mujacic, M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22, 1399-1408.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 2
    • 0029555566 scopus 로고
    • Formation of inclusion bodies may be the key factor for the stability of expressed products in E. coli
    • Wei, G.; Tang, J. C. Formation of inclusion bodies may be the key factor for the stability of expressed products in E. coli. Biochem. Mol. Biol. 1995, 37, 895-911.
    • (1995) Biochem. Mol. Biol. , vol.37 , pp. 895-911
    • Wei, G.1    Tang, J.C.2
  • 4
    • 0031157025 scopus 로고    scopus 로고
    • Molecular Chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli
    • Thomas, J. G.; Ayling, A.; Baneyx, F. Molecular Chaperones, Folding Catalysts, and the Recovery of Active Recombinant Proteins from E. coli. Appl. Biochem. Biotech. 1997, 66, 197-238.
    • (1997) Appl. Biochem. Biotech. , vol.66 , pp. 197-238
    • Thomas, J.G.1    Ayling, A.2    Baneyx, F.3
  • 5
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ- GroE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Eschericia coli
    • Nishihara, K. Chaperone Coexpression Plasmids: Differential and Synergistic Roles of DnaK-DnaJ- GroE and GroEL-GroES in Assisting Folding of an Allergen of Japanese Cedar Pollen, Cryj2, in Eschericia coli. Appl. Environ. Microbiol. 1998, 64, 1694-1699.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1694-1699
    • Nishihara, K.1
  • 6
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • Hammarström, M.; Hellgren, N.; van Den Berg, S.; Berglund, H.; Hard, T. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 2002, 11, 313-321.
    • (2002) Protein Sci. , vol.11 , pp. 313-321
    • Hammarström, M.1    Hellgren, N.2    Van Den Berg, S.3    Berglund, H.4    Hard, T.5
  • 7
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • Davis, G. D.; Elisee, C.; Newham, D. M.; Harrison, R. G. New Fusion Protein Systems Designed to Give Soluble Expression in Escherichia coli. Biotechnol. Bioeng. 1999, 65, 382-388.
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 8
    • 9344234999 scopus 로고    scopus 로고
    • Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion
    • Trabbic-Carlson, K.; Liu, L.; Kim, B.; Chilkoti, A. Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion. Protein Sci. 2004, 13, 3274-3284.
    • (2004) Protein Sci. , vol.13 , pp. 3274-3284
    • Trabbic-Carlson, K.1    Liu, L.2    Kim, B.3    Chilkoti, A.4
  • 9
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe, K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 2003, 60, 523-533.
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 523-533
    • Terpe, K.1
  • 11
    • 0029543755 scopus 로고    scopus 로고
    • Propeptide-mediated folding in subtilisin: The intramolecular chaperone concept
    • Shinde, U.; Inouye, M. Propeptide-mediated folding in subtilisin: the intramolecular chaperone concept. Adv. Exp. Med. Biol. 1996, 379, 147-154.
    • (1996) Adv. Exp. Med. Biol. , vol.379 , pp. 147-154
    • Shinde, U.1    Inouye, M.2
  • 13
    • 0021167693 scopus 로고
    • Clostridium thermocellum: Adhesion and sporulation while adhered to cellulose and hemicellulose
    • Wiegel, J.; Dykstra, M. Clostridium thermocellum: adhesion and sporulation while adhered to cellulose and hemicellulose. Appl. Microbiol. Biotechnol. 1984, 20, 59-65.
    • (1984) Appl. Microbiol. Biotechnol. , vol.20 , pp. 59-65
    • Wiegel, J.1    Dykstra, M.2
  • 16
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E. L.; Eddy, S. R.; Durbin, R. Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins 1997, 28, 405-420.
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 17
    • 0025953577 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • Wilkinson, D. L.; Harrison, R. G. Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology 1991, 9, 443-448.
    • (1991) Biotechnology , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 18
    • 0033676098 scopus 로고    scopus 로고
    • DNA cloning using in vitro site-specific recombination
    • Hartley, J. L.; Temple, G. F.; Brasch, M. A. DNA Cloning Using in vitro Site-Specific Recombination. Genome Res. 2000, 10, 1788-1795.
    • (2000) Genome Res. , vol.10 , pp. 1788-1795
    • Hartley, J.L.1    Temple, G.F.2    Brasch, M.A.3
  • 21
    • 3543050105 scopus 로고    scopus 로고
    • His tag effect on solubility of human proteins produced in Escherichia coli: A comparison between four expression vectors
    • Woestenenk, E. A.; Hammarström, M.; van den Berg, S.; Härd, T.; Berglund, H. His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors. J. Struct. Funct. Genomics 2004, 5, 217-229.
    • (2004) J. Struct. Funct. Genomics , vol.5 , pp. 217-229
    • Woestenenk, E.A.1    Hammarström, M.2    Van Den Berg, S.3    Härd, T.4    Berglund, H.5
  • 22
    • 0037438709 scopus 로고    scopus 로고
    • Physical-chemical features of nondetergent sulfobetaines active as protein-folding helpers
    • Expert-Bezancon, N.; Rabilloud, T.; Vuillard, L.; Goldberg, M. E. Physical-chemical features of nondetergent sulfobetaines active as protein-folding helpers. Biophys. Chem. 2003, 100, 469-479.
    • (2003) Biophys. Chem. , vol.100 , pp. 469-479
    • Expert-Bezancon, N.1    Rabilloud, T.2    Vuillard, L.3    Goldberg, M.E.4
  • 23
    • 0033065348 scopus 로고    scopus 로고
    • Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli
    • Vonrhein, C.; Schmidt, U.; Ziegler, G. A.; Schweiger, S.; Hanukoglu, I.; Schulz, G. E. Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli. FEBS Lett. 1999, 443, 167-169.
    • (1999) FEBS Lett. , vol.443 , pp. 167-169
    • Vonrhein, C.1    Schmidt, U.2    Ziegler, G.A.3    Schweiger, S.4    Hanukoglu, I.5    Schulz, G.E.6
  • 24
    • 29144461245 scopus 로고    scopus 로고
    • Immunoprecipitation with Penta-His antibody
    • Steinert, K.; Wulbeck, M.; Ribbe, J. Immunoprecipitation with Penta-His antibody. QIAGEN News 1998, 2, 20.
    • (1998) QIAGEN News , vol.2 , pp. 20
    • Steinert, K.1    Wulbeck, M.2    Ribbe, J.3
  • 25
    • 14144255127 scopus 로고    scopus 로고
    • Understanding the relationship between the primary structure of proteins and the propensity to be soluble on overexpression in Escherichia coli
    • Idicula-Thomas, S.; Balaji, P. V. Understanding the relationship between the primary structure of proteins and the propensity to be soluble on overexpression in Escherichia coli. Protein Sci. 2005, 14, 582-592.
    • (2005) Protein Sci. , vol.14 , pp. 582-592
    • Idicula-Thomas, S.1    Balaji, P.V.2
  • 26
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S.; Tsai, C.-J.; Russinov, R. Factors enhancing protein thermostability. Prot. Eng. 2000, 13, 179-191.
    • (2000) Prot. Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.-J.2    Russinov, R.3
  • 27
    • 4143060688 scopus 로고    scopus 로고
    • Improved stability of a protein vaccine through elimination of a partially unfolded state
    • McHugh, C. A.; Tammariello, R. F.; Millard, C. B.; Carra, J. H. Improved stability of a protein vaccine through elimination of a partially unfolded state. Protein Sci. 2004, 13, 2736-2743.
    • (2004) Protein Sci. , vol.13 , pp. 2736-2743
    • McHugh, C.A.1    Tammariello, R.F.2    Millard, C.B.3    Carra, J.H.4
  • 29
    • 0034855858 scopus 로고    scopus 로고
    • How do thermophilic proteins deal with heat?
    • Kumar, S.; Nussinov, R. How do thermophilic proteins deal with heat? Cell. Mol. Life Sci. 2001, 8, 1216-1233.
    • (2001) Cell. Mol. Life Sci. , vol.8 , pp. 1216-1233
    • Kumar, S.1    Nussinov, R.2
  • 30
    • 0033433951 scopus 로고    scopus 로고
    • Human liver mitochondrial aldehyde dehydrogenase: Three-dimensional structure and the restoration of solubility and activity of chimeric forms
    • Ni, L.; Zhou, J.; Hurley, T. D.; Weiner, H. Human liver mitochondrial aldehyde dehydrogenase: Three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999, 8, 2784-2790.
    • (1999) Protein Sci. , vol.8 , pp. 2784-2790
    • Ni, L.1    Zhou, J.2    Hurley, T.D.3    Weiner, H.4
  • 31
    • 0033485411 scopus 로고    scopus 로고
    • Effect of foreign N-terminal residues on the conformational stability of human lysozyme
    • Takano, K.; Tsuchimori, K.; Yamagata, Y.: Yutani, K. Effect of foreign N-terminal residues on the conformational stability of human lysozyme. Eur. J. Biochem. 1999, 266, 675-682.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 675-682
    • Takano, K.1    Tsuchimori, K.2    Yamagata, Y.3    Yutani, K.4
  • 32
    • 1642348275 scopus 로고    scopus 로고
    • Effect of signal peptide on the stability and folding kinetics of maltose-binding protein
    • Beena, K.; Udgaonkar, J. B.; Varadarajan, R. Effect of signal peptide on the stability and folding kinetics of maltose-binding protein. Biochemistry 2004, 43, 3608-3619.
    • (2004) Biochemistry , vol.43 , pp. 3608-3619
    • Beena, K.1    Udgaonkar, J.B.2    Varadarajan, R.3
  • 33
    • 0029879607 scopus 로고    scopus 로고
    • Phylogenetic occurrence of coiled coil proteins: Implications for tissue structure in metazoa via a coiled coil tissue matrix
    • Odgren, P. R.; Harvie, L. W., Jr.; Fey, E. G. Phylogenetic occurrence of coiled coil proteins: Implications for tissue structure in metazoa via a coiled coil tissue matrix. Proteins: Struct., Funct., Genet. 1998, 24, 467-484.
    • (1998) Proteins: Struct., Funct., Genet. , vol.24 , pp. 467-484
    • Odgren, P.R.1    Harvie Jr., L.W.2    Fey, E.G.3
  • 34
    • 0021766036 scopus 로고
    • The C-terminus of bacteriorodopsin is a random coil
    • Wallace, B. A.; Kohl, N. The C-terminus of bacteriorodopsin is a random coil. BBA 1984, 17, 93-98.
    • (1984) BBA , vol.17 , pp. 93-98
    • Wallace, B.A.1    Kohl, N.2
  • 35
  • 36
    • 9244260521 scopus 로고    scopus 로고
    • Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides
    • Nguyen, H. D.; Hall, C. K. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. PNAS 2004, 101, 16180-16185.
    • (2004) PNAS , vol.101 , pp. 16180-16185
    • Nguyen, H.D.1    Hall, C.K.2
  • 37
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for the amyloid fibrillation: The importance of being unfolded
    • Uversky, V. N.; Fink, A. L. Conformational constraints for the amyloid fibrillation: The importance of being unfolded. Biochim. Biophys. Acta 2004, 1698, 131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 38
    • 4143060688 scopus 로고    scopus 로고
    • Improved stability of a protein vaccine through elimination of a partially unfolded state
    • McHugh, C. A.; Tammariello, R. F.; Millard, C. B.; Carra, J. H. Improved stability of a protein vaccine through elimination of a partially unfolded state. Protein Science 2004, 13, 2736-2743.
    • (2004) Protein Science , vol.13 , pp. 2736-2743
    • McHugh, C.A.1    Tammariello, R.F.2    Millard, C.B.3    Carra, J.H.4
  • 39
    • 0020655246 scopus 로고
    • Structural domains in protein and their role in the dynamics of protein function
    • Janin, J.; Wodak, S. J. Structural domains in protein and their role in the dynamics of protein function. Prog. Biophys. Mol. Biol. 1983, 42, 21-78.
    • (1983) Prog. Biophys. Mol. Biol. , vol.42 , pp. 21-78
    • Janin, J.1    Wodak, S.J.2
  • 40
    • 2342460338 scopus 로고    scopus 로고
    • From hyperthermophiles to psychrophiles: The structural basis of temperature stability of the amino acid dehydrogenases
    • Baker, P. J. From hyperthermophiles to psychrophiles: the structural basis of temperature stability of the amino acid dehydrogenases. Biochem. Soc. Trans. 2004, 32, 264-268.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 264-268
    • Baker, P.J.1
  • 42
    • 0019287872 scopus 로고
    • Thermostability and aliphatic index of globular proteins
    • Ikai, A. Thermostability and aliphatic index of globular proteins. J. Biochem. 1980, 88, 1895-1898.
    • (1980) J. Biochem. , vol.88 , pp. 1895-1898
    • Ikai, A.1
  • 43
    • 0003613070 scopus 로고    scopus 로고
    • A comparison of amino acid composition of proteins from thermophiles and mesophiles
    • Lu, B.; Wang, G.; Huang, P. A comparison of amino acid composition of proteins from thermophiles and mesophiles. Wei Sheng Wu Xue Boo 1998, 38, 20-25.
    • (1998) Wei Sheng Wu Xue Boo , vol.38 , pp. 20-25
    • Lu, B.1    Wang, G.2    Huang, P.3
  • 44
    • 0019856479 scopus 로고
    • Protein thermostability. Correlations between calculated microscopic parameters and growth temperatures for closely related thermophilic and mesophilic bacilli
    • Merkler, D. J.; Farrington, G. K.; Wedler, F. C. Protein thermostability. Correlations between calculated microscopic parameters and growth temperatures for closely related thermophilic and mesophilic bacilli. Int. J. Pept. Res. 1981, 18, 430-442.
    • (1981) Int. J. Pept. Res. , vol.18 , pp. 430-442
    • Merkler, D.J.1    Farrington, G.K.2    Wedler, F.C.3
  • 45
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies
    • Bach, H.; Mazor, Y.; Shaky, S.; Berdichevsky, A. S.-L. Y.; Gutnick, D. L.; Benhar, I. Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies. J. Mol. Biol. 2001, 312, 79-93.
    • (2001) J. Mol. Biol. , vol.312 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3    Berdichevsky, A.S.-L.Y.4    Gutnick, D.L.5    Benhar, I.6
  • 46
    • 0035104597 scopus 로고    scopus 로고
    • Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins
    • Fox, J. D.; Kapust, R. B.; Waugh, D. S. Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins. Protein Sci. 2001, 10, 622-530.
    • (2001) Protein Sci. , vol.10 , pp. 622-530
    • Fox, J.D.1    Kapust, R.B.2    Waugh, D.S.3
  • 47
    • 0030978479 scopus 로고    scopus 로고
    • Thermodynamic characterization of the reversible, two-state unfolding of maltose-binding protein, a large two-domain protein
    • Ganesh, C.; Shah, A. N.; Swaminathan, C. P.; Surolia A.; Varadarajan, R. Thermodynamic characterization of the reversible, two-state unfolding of maltose-binding protein, a large two-domain protein. Biochemistry 1997, 36, 5020-5028.
    • (1997) Biochemistry , vol.36 , pp. 5020-5028
    • Ganesh, C.1    Shah, A.N.2    Swaminathan, C.P.3    Surolia, A.4    Varadarajan, R.5


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