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Volumn 109, Issue 1-2, 2004, Pages 45-52

Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning

Author keywords

Chaperones; Co expression; E. coli; Recombinant proteins; Vectors

Indexed keywords

BACTERIA; METABOLISM; OPTIMIZATION; PROTEINS; TOXIC MATERIALS;

EID: 1842582929     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2003.10.025     Document Type: Conference Paper
Times cited : (65)

References (17)
  • 1
    • 0028798788 scopus 로고
    • Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL
    • Amrein K.E., Takacs B., Stieger M., Molnos J., Flint N.A., Burn P. Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL. Proc. Natl. Acad. Sci. U.S.A. 92:1995;1048-1052.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1048-1052
    • Amrein, K.E.1    Takacs, B.2    Stieger, M.3    Molnos, J.4    Flint, N.A.5    Burn, P.6
  • 2
    • 0026498778 scopus 로고
    • Physiological consequences of DnaK and DnaJ overproduction in Escherichia coli
    • Blum P., Ory J., Bauernfeind J., Krska J. Physiological consequences of DnaK and DnaJ overproduction in Escherichia coli. J. Bacteriol. 174:1992;7436-7444.
    • (1992) J. Bacteriol. , vol.174 , pp. 7436-7444
    • Blum, P.1    Ory, J.2    Bauernfeind, J.3    Krska, J.4
  • 3
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., 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
  • 4
    • 0035951410 scopus 로고    scopus 로고
    • Protein aggregation as bacterial inclusion bodies is reversible
    • Carriò M.M., Villaverde A. Protein aggregation as bacterial inclusion bodies is reversible. FEBS Lett. 489:2001;29-33.
    • (2001) FEBS Lett. , vol.489 , pp. 29-33
    • Carriò, M.M.1    Villaverde, A.2
  • 5
    • 0031543319 scopus 로고    scopus 로고
    • A set of pBR322-compatible plasmids allowing the testing of chaperone-assisted folding of proteins overexpressed in Escherichia coli
    • Castanié M.-P., Berges H., Oreglia J., Prere M.F., Fayet O. A set of pBR322-compatible plasmids allowing the testing of chaperone-assisted folding of proteins overexpressed in Escherichia coli. Anal. Biochem. 254:1997;150-152.
    • (1997) Anal. Biochem. , vol.254 , pp. 150-152
    • Castanié, M.-P.1    Berges, H.2    Oreglia, J.3    Prere, M.F.4    Fayet, O.5
  • 6
    • 0033810061 scopus 로고    scopus 로고
    • Recombinant maize protoporphyrinogen IX oxidase expressed in Escherichia coli forms complexes with GroEL and DnaK chaperones
    • de Marco A., Volrath S., Bruyere T., Law M., Fonnè-Pfister R. Recombinant maize protoporphyrinogen IX oxidase expressed in Escherichia coli forms complexes with GroEL and DnaK chaperones. Prot. Exp. Purif. 20:2000;81-86.
    • (2000) Prot. Exp. Purif. , vol.20 , pp. 81-86
    • De Marco, A.1    Volrath, S.2    Bruyere, T.3    Law, M.4    Fonnè-Pfister, R.5
  • 7
    • 0035796504 scopus 로고    scopus 로고
    • Analysis of heterodimer formation by Xklp3A/B, a newly cloned kinesin-II from Xenopus laevis
    • De Marco V., Burkhard P., Le Bot N., Vernos I., Hoenger A. Analysis of heterodimer formation by Xklp3A/B, a newly cloned kinesin-II from Xenopus laevis. EMBO J. 20:2001;3370-3379.
    • (2001) EMBO J. , vol.20 , pp. 3370-3379
    • De Marco, V.1    Burkhard, P.2    Le Bot, N.3    Vernos, I.4    Hoenger, A.5
  • 8
    • 0035810693 scopus 로고    scopus 로고
    • The metabolic burden of the PGK1 and ADH2 promoter systems for the heterologous xylanase production by Saccharomyces cerevisiae in defined medium
    • Görgens J.F., van Zyl W.H., Knoetze J.H., Hahn-Hägerdal B. The metabolic burden of the PGK1 and ADH2 promoter systems for the heterologous xylanase production by Saccharomyces cerevisiae in defined medium. Biotechnol. Bioeng. 73:2001;238-245.
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 238-245
    • Görgens, J.F.1    Van Zyl, W.H.2    Knoetze, J.H.3    Hahn-Hägerdal, B.4
  • 9
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • Hanning G., Makrides S.C. Strategies for optimizing heterologous protein expression in Escherichia coli. Tibtechnology. 16:1998;54-60.
    • (1998) Tibtechnology , vol.16 , pp. 54-60
    • Hanning, G.1    Makrides, S.C.2
  • 11
    • 0031026329 scopus 로고    scopus 로고
    • Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides
    • Kandror O., Sherman M., Moerschell R., Goldberg A.L. Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides. J. Biol. Chem. 272:1997;1730-1734.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1730-1734
    • Kandror, O.1    Sherman, M.2    Moerschell, R.3    Goldberg, A.L.4
  • 12
    • 1842470075 scopus 로고    scopus 로고
    • Physiological responses to heterologous protein production at the translational level
    • Poster L17, EFB Conference, Cernobbio, Italy.
    • Pedersen, P.A., Steffensen, L., 2002. Physiological responses to heterologous protein production at the translational level. In: Recombinant Protein Production with Prokaryotic and Eukaryotic Cells, Poster L17, EFB Conference, Cernobbio, Italy.
    • (2002) Recombinant Protein Production with Prokaryotic and Eukaryotic Cells
    • Pedersen, P.A.1    Steffensen, L.2
  • 13
    • 1842522185 scopus 로고    scopus 로고
    • Cellular responses to secretion stress in the filamentous fungus Trichoderma reesei
    • Saloheimo M., Pakula T., Valkonen M., Penttilä M. Cellular responses to secretion stress in the filamentous fungus Trichoderma reesei. EFB Event. 112:2002;L14.
    • (2002) EFB Event , vol.112 , pp. 14
    • Saloheimo, M.1    Pakula, T.2    Valkonen, M.3    Penttilä, M.4
  • 15
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • Tan S. A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli. Prot. Exp. Purif. 21:2001;224-234.
    • (2001) Prot. Exp. Purif. , vol.21 , pp. 224-234
    • Tan, S.1
  • 16
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperone and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu T., Mogk A., Langen H., Goloubinoff P., Bukau B. Genetic dissection of the roles of chaperone and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol. Microb. 40:2001;397-413.
    • (2001) Mol. Microb. , vol.40 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 17
    • 0037027392 scopus 로고    scopus 로고
    • Metabolic adaptation of Escherichia coli during temperature-induced recombination protein production. 2. Redirection of metabolic fluxes
    • Weber J., Hoffmann F., Rinas U. Metabolic adaptation of Escherichia coli during temperature-induced recombination protein production. 2. Redirection of metabolic fluxes. Biotechnol. Bioeng. 80:2002;320-330.
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 320-330
    • Weber, J.1    Hoffmann, F.2    Rinas, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.