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Volumn 110, Issue , 2015, Pages 159-164

Positional effects of fusion partners on the yield and solubility of MBP fusion proteins

Author keywords

Fusion protein; Gateway cloning; Inclusion bodies; MBP; Solubility enhancer

Indexed keywords

ESCHERICHIA COLI;

EID: 84925411269     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2015.03.004     Document Type: Article
Times cited : (39)

References (20)
  • 1
    • 84897604263 scopus 로고    scopus 로고
    • Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: The novel Fh8 system
    • S. Costa, A. Almeida, A. Castro, and L. Domingues Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system Front. Microbiol. 5 2014 63
    • (2014) Front. Microbiol. , vol.5 , pp. 63
    • Costa, S.1    Almeida, A.2    Castro, A.3    Domingues, L.4
  • 2
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • D. Esposito, and D.K. Chatterjee Enhancement of soluble protein expression through the use of fusion tags Curr. Opin. Biotechnol. 17 2006 353 358
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 3
    • 80052624922 scopus 로고    scopus 로고
    • Expression of proteins in Escherichia coli as fusions with maltose-binding protein to rescue non-expressed targets in a high-throughput protein-expression and purification pipeline
    • S.N. Hewitt, R. Choi, A. Kelley, G.J. Crowther, A.J. Napuli, and W.C. Van Voorhis Expression of proteins in Escherichia coli as fusions with maltose-binding protein to rescue non-expressed targets in a high-throughput protein-expression and purification pipeline Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 2011 1006 1009
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.67 , pp. 1006-1009
    • Hewitt, S.N.1    Choi, R.2    Kelley, A.3    Crowther, G.J.4    Napuli, A.J.5    Van Voorhis, W.C.6
  • 4
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • R.B. Kapust, and D.S. Waugh Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci. 8 1999 1668 1674
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 5
    • 20744445059 scopus 로고    scopus 로고
    • Escherichia coli fusion carrier proteins act as solubilizing agents for recombinant uncoupling protein 1 through interactions with GroEL
    • P. Douette, R. Navet, P. Gerkens, M. Galleni, D. Levy, and F.E. Sluse Escherichia coli fusion carrier proteins act as solubilizing agents for recombinant uncoupling protein 1 through interactions with GroEL Biochem. Biophys. Res. Commun. 333 2005 686 693
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 686-693
    • Douette, P.1    Navet, R.2    Gerkens, P.3    Galleni, M.4    Levy, D.5    Sluse, F.E.6
  • 6
    • 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
    • J.D. Fox, R.B. Kapust, and D.S. Waugh 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. 10 2001 622 630
    • (2001) Protein Sci. , vol.10 , pp. 622-630
    • Fox, J.D.1    Kapust, R.B.2    Waugh, D.S.3
  • 7
    • 0037468510 scopus 로고    scopus 로고
    • Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers
    • J.D. Fox, K.M. Routzahn, M.H. Bucher, and D.S. Waugh Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers FEBS Lett. 537 2003 53 57
    • (2003) FEBS Lett. , vol.537 , pp. 53-57
    • Fox, J.D.1    Routzahn, K.M.2    Bucher, M.H.3    Waugh, D.S.4
  • 8
    • 28844481147 scopus 로고    scopus 로고
    • Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners
    • S. Nallamsetty, and D.S. Waugh Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners Protein Expr. Purif. 45 2006 175 182
    • (2006) Protein Expr. Purif. , vol.45 , pp. 175-182
    • Nallamsetty, S.1    Waugh, D.S.2
  • 9
    • 35648941605 scopus 로고    scopus 로고
    • Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins
    • S. Nallamsetty, and D.S. Waugh Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins Biochem. Biophys. Res. Commun. 364 2007 639 644
    • (2007) Biochem. Biophys. Res. Commun. , vol.364 , pp. 639-644
    • Nallamsetty, S.1    Waugh, D.S.2
  • 10
    • 84869205433 scopus 로고    scopus 로고
    • The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediated
    • S. Raran-Kurussi, and D.S. Waugh The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediated PLoS ONE 7 2012 e49589
    • (2012) PLoS ONE , vol.7 , pp. e49589
    • Raran-Kurussi, S.1    Waugh, D.S.2
  • 11
  • 12
    • 0032571132 scopus 로고    scopus 로고
    • Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli
    • D. Sachdev, and J.M. Chirgwin Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli Biochem. Biophys. Res. Commun. 244 1998 933 937
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 933-937
    • Sachdev, D.1    Chirgwin, J.M.2
  • 13
    • 13244265563 scopus 로고    scopus 로고
    • Production of soluble mammalian proteins in Escherichia coli: Identification of protein features that correlate with successful expression
    • M.R. Dyson, S.P. Shadbolt, K.J. Vincent, R.L. Perera, and J. McCafferty Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression BMC Biotechnol. 4 2004 32
    • (2004) BMC Biotechnol. , vol.4 , pp. 32
    • Dyson, M.R.1    Shadbolt, S.P.2    Vincent, K.J.3    Perera, R.L.4    McCafferty, J.5
  • 14
    • 70349582984 scopus 로고    scopus 로고
    • Overproduction, purification and structure determination of human dual-specificity phosphatase 14
    • G.T. Lountos, J.E. Tropea, S. Cherry, and D.S. Waugh Overproduction, purification and structure determination of human dual-specificity phosphatase 14 Acta Crystallogr. D Biol. Crystallogr. 65 2009 1013 1020
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 1013-1020
    • Lountos, G.T.1    Tropea, J.E.2    Cherry, S.3    Waugh, D.S.4
  • 15
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • R.B. Kapust, J. Tozser, J.D. Fox, D.E. Anderson, S. Cherry, T.D. Copeland, and D.S. Waugh Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency Protein Eng. 14 2001 993 1000
    • (2001) Protein Eng. , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 17
    • 28844475180 scopus 로고    scopus 로고
    • Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli
    • S. Nallamsetty, B.P. Austin, K.J. Penrose, and D.S. Waugh Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli Protein Sci. 14 2005 2964 2971
    • (2005) Protein Sci. , vol.14 , pp. 2964-2971
    • Nallamsetty, S.1    Austin, B.P.2    Penrose, K.J.3    Waugh, D.S.4
  • 19
    • 0242401865 scopus 로고    scopus 로고
    • High-resolution structure of the Yersinia pestis protein tyrosine phosphatase YopH in complex with a phosphotyrosyl mimetic-containing hexapeptide
    • J. Phan, K. Lee, S. Cherry, J.E. Tropea, T.R. Burke Jr., and D.S. Waugh High-resolution structure of the Yersinia pestis protein tyrosine phosphatase YopH in complex with a phosphotyrosyl mimetic-containing hexapeptide Biochemistry 42 2003 13113 13121
    • (2003) Biochemistry , vol.42 , pp. 13113-13121
    • Phan, J.1    Lee, K.2    Cherry, S.3    Tropea, J.E.4    Burke, Jr.T.R.5    Waugh, D.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.