메뉴 건너뛰기




Volumn 52, Issue 2, 2007, Pages 280-285

Effect of osmotic stress and heat shock in recombinant protein overexpression and crystallization

Author keywords

Crystallization; Osmotic stress; Recombinant protein; Solubility

Indexed keywords

RECOMBINANT PROTEIN;

EID: 33846459989     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.09.015     Document Type: Article
Times cited : (90)

References (31)
  • 1
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 10 (1999) 411-421
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 3
    • 32344437870 scopus 로고    scopus 로고
    • Production of Lewis tetrasaccharides by metabolically engineered Escherichia coli
    • Dumon C., Bosso C., Utille J.P., Heyrand A., and Samain E. Production of Lewis tetrasaccharides by metabolically engineered Escherichia coli. Chembiochem. 7 (2006) 359-365
    • (2006) Chembiochem. , vol.7 , pp. 359-365
    • Dumon, C.1    Bosso, C.2    Utille, J.P.3    Heyrand, A.4    Samain, E.5
  • 4
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sorensen H.P., and Mortensen K.K. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microbiol Cell Factories 4 (2005) 1
    • (2005) Microbiol Cell Factories , vol.4 , pp. 1
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 5
    • 0031719418 scopus 로고    scopus 로고
    • Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments
    • Kempf B., and Bremer E. Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments. Arch. Microbiol. 170 (1998) 319-330
    • (1998) Arch. Microbiol. , vol.170 , pp. 319-330
    • Kempf, B.1    Bremer, E.2
  • 6
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., and Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92 (1998) 351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 7
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 (2004) 1399-1408
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 8
    • 0346935999 scopus 로고    scopus 로고
    • DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli
    • Chen Y., Song J., Sui S.F., and Wang D.N. DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli. Protein Expr. Purif. 32 (2003) 221-231
    • (2003) Protein Expr. Purif. , vol.32 , pp. 221-231
    • Chen, Y.1    Song, J.2    Sui, S.F.3    Wang, D.N.4
  • 9
    • 0036417347 scopus 로고    scopus 로고
    • Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain fv antibodies in Escherichia coli
    • Zhang Z., Li Z.H., Wang F., Fang M., Yin C.C., Zhou Z.Y., Lin Q., and Huang H.L. Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain fv antibodies in Escherichia coli. Protein Expr. Purif. 26 (2002) 218-228
    • (2002) Protein Expr. Purif. , vol.26 , pp. 218-228
    • Zhang, Z.1    Li, Z.H.2    Wang, F.3    Fang, M.4    Yin, C.C.5    Zhou, Z.Y.6    Lin, Q.7    Huang, H.L.8
  • 10
    • 0035715182 scopus 로고    scopus 로고
    • Expression of recombinant zeta-crystallin in Escherichia coli with the help of GroEL/ES and its purification
    • Goenca S., and Rao C.M. Expression of recombinant zeta-crystallin in Escherichia coli with the help of GroEL/ES and its purification. Protein Expr. Purif. 21 (2001) 260-267
    • (2001) Protein Expr. Purif. , vol.21 , pp. 260-267
    • Goenca, S.1    Rao, C.M.2
  • 11
    • 27644571313 scopus 로고    scopus 로고
    • Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system
    • Liu Y., Zhao T.-J., Yan Y.-B., and Zhou H.-M. Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Protein Expr. Purif. 44 (2005) 155-161
    • (2005) Protein Expr. Purif. , vol.44 , pp. 155-161
    • Liu, Y.1    Zhao, T.-J.2    Yan, Y.-B.3    Zhou, H.-M.4
  • 12
  • 13
    • 15844395096 scopus 로고
    • Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins
    • Thomas J., and Baneyx F. Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins. J. Biol. Chem. 271 (1995) 11141-11147
    • (1995) J. Biol. Chem. , vol.271 , pp. 11141-11147
    • Thomas, J.1    Baneyx, F.2
  • 14
    • 0033167089 scopus 로고    scopus 로고
    • Protein synthesis inhibitors and ethanol selectively enhance heterologous expression of P450s and related proteins in Escherichia coli
    • Kusano K., Waterman M.R., Sakaguchi M., Omura T., and Kagawa N. Protein synthesis inhibitors and ethanol selectively enhance heterologous expression of P450s and related proteins in Escherichia coli. Arch. Biochem. Biophys. 367 (1999) 129-136
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 129-136
    • Kusano, K.1    Waterman, M.R.2    Sakaguchi, M.3    Omura, T.4    Kagawa, N.5
  • 15
    • 0348224028 scopus 로고    scopus 로고
    • Tight binding of deoxyribonucleotide triphosphates to human thymidine kinase 2 expressed in Escherichia coli
    • Barosso J.F., Elholm M., and Flatmark T. Tight binding of deoxyribonucleotide triphosphates to human thymidine kinase 2 expressed in Escherichia coli. Biochemistry 42 (2003) 15158-15169
    • (2003) Biochemistry , vol.42 , pp. 15158-15169
    • Barosso, J.F.1    Elholm, M.2    Flatmark, T.3
  • 17
    • 0032755251 scopus 로고    scopus 로고
    • Manipulating the amyloid-beta aggregation pathway with chemical chaperones
    • Yang D.S., Yip C.M., Huang T.H., Chakrabartty A., and Fraser P.E. Manipulating the amyloid-beta aggregation pathway with chemical chaperones. J. Biol. Chem. 274 (1999) 32970-32974
    • (1999) J. Biol. Chem. , vol.274 , pp. 32970-32974
    • Yang, D.S.1    Yip, C.M.2    Huang, T.H.3    Chakrabartty, A.4    Fraser, P.E.5
  • 18
    • 0034490988 scopus 로고    scopus 로고
    • Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement
    • Voziyan P.A., and Fisher M.T. Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement. Protein Sci. 9 (2000) 2405-2412
    • (2000) Protein Sci. , vol.9 , pp. 2405-2412
    • Voziyan, P.A.1    Fisher, M.T.2
  • 19
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: natural selection of a thermodynamic force in protein folding
    • Bolen D.W., and Baskakov I.V. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 310 (2001) 955-963
    • (2001) J. Mol. Biol. , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 20
    • 3142619246 scopus 로고    scopus 로고
    • Mutational and structural-based analyses of the osmolyte effect on protein stability
    • Takano K., Saito M., Morikawa M., and Kanaya S. Mutational and structural-based analyses of the osmolyte effect on protein stability. J. Biochem. 135 (2004) 701-708
    • (2004) J. Biochem. , vol.135 , pp. 701-708
    • Takano, K.1    Saito, M.2    Morikawa, M.3    Kanaya, S.4
  • 21
    • 0026327753 scopus 로고
    • novel strategy for production of a highly expressed recombinant protein in an active form
    • Blakwell J.R., and A Horgan R. novel strategy for production of a highly expressed recombinant protein in an active form. FEBS 295 (1991) 10-12
    • (1991) FEBS , vol.295 , pp. 10-12
    • Blakwell, J.R.1    A Horgan, R.2
  • 22
    • 11844256960 scopus 로고    scopus 로고
    • Expression and purification of histidine-tagged bacteriophage T7 DNA polymerase
    • Schlicke M., and Brakmann S. Expression and purification of histidine-tagged bacteriophage T7 DNA polymerase. Protein Expr. Purif. 39 (2005) 247-253
    • (2005) Protein Expr. Purif. , vol.39 , pp. 247-253
    • Schlicke, M.1    Brakmann, S.2
  • 23
    • 29144469368 scopus 로고    scopus 로고
    • Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    • de Marco A., Vigh L., Diamant S., and Goloubinoff P. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. Cell Stress Chaperones 10 (2005) 329-339
    • (2005) Cell Stress Chaperones , vol.10 , pp. 329-339
    • de Marco, A.1    Vigh, L.2    Diamant, S.3    Goloubinoff, P.4
  • 24
    • 0035955743 scopus 로고    scopus 로고
    • Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses
    • Diamant S., Eliahu N., Rosenthal D., and Goloubinoff P. Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J. Biol. Chem. 276 (2001) 39586-39591
    • (2001) J. Biol. Chem. , vol.276 , pp. 39586-39591
    • Diamant, S.1    Eliahu, N.2    Rosenthal, D.3    Goloubinoff, P.4
  • 25
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C., and de Jong P.J. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18 (1990) 6069-6074
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 27
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier F.W. Protein production by auto-induction in high-density shaking cultures. Protein Expr. Purif. 41 (2005) 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 28
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276 (1997) 523-529
    • (1997) Methods Enzymol. , vol.276 , pp. 523-529
    • Doublie, S.1
  • 29
    • 0026206788 scopus 로고
    • Sparse matrix sampling: a screening method for crystallization of proteins
    • Jancarik J., and Kim S.-H. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24 (1991) 409-411
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 30
    • 11344287184 scopus 로고    scopus 로고
    • Crystal structure of the conserved hypothetical protein MPN330 (GI: 1674200) from Mycoplasma pneumoniae
    • Das D., Oganesyan N., Yokota H., Pufan R., Kim R., and Kim S.-H. Crystal structure of the conserved hypothetical protein MPN330 (GI: 1674200) from Mycoplasma pneumoniae. Proteins Struct. Funct. Bioinform. 58 (2005) 504-508
    • (2005) Proteins Struct. Funct. Bioinform. , vol.58 , pp. 504-508
    • Das, D.1    Oganesyan, N.2    Yokota, H.3    Pufan, R.4    Kim, R.5    Kim, S.-H.6
  • 31
    • 0024033825 scopus 로고
    • The effect of sugars on β-lactamase aggregation in Escherichia coli
    • Bowden A., and Georgiou G. The effect of sugars on β-lactamase aggregation in Escherichia coli. Biotechnol. Prog. 4 (1988) 97-101
    • (1988) Biotechnol. Prog. , vol.4 , pp. 97-101
    • Bowden, A.1    Georgiou, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.