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Volumn 224, Issue 1-2, 1998, Pages 45-52

High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage Lambda head protein D

Author keywords

Expression vector; Fusion protein; Gene fusion; Inclusion bodies; Protein expression; Protein Stability

Indexed keywords

BACTERIAL PROTEIN; CAPSID PROTEIN; CYSTEINE; HYBRID PROTEIN;

EID: 0032509329     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00538-1     Document Type: Article
Times cited : (67)

References (30)
  • 1
    • 0030272645 scopus 로고    scopus 로고
    • Protein expression using ubiquitin fusion and cleavage
    • Baker R.T. Protein expression using ubiquitin fusion and cleavage. Curr. Opin. Biotechnol. 7:1996;541-546.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 541-546
    • Baker, R.T.1
  • 2
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Dérijard B., Hibi M., Wu I.H., Barrett T., Su B., Deng T., Karin M., Davis R.J. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell. 76:1994;1025-1037.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Dérijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 3
    • 0027366430 scopus 로고
    • Structural transitions during maturation of bacteriophage lambda capsids
    • Dokland T., Murialdo H. Structural transitions during maturation of bacteriophage lambda capsids. J. Mol. Biol. 233:1993;682-694.
    • (1993) J. Mol. Biol. , vol.233 , pp. 682-694
    • Dokland, T.1    Murialdo, H.2
  • 4
    • 0028243505 scopus 로고
    • C-Abl kinase regulates the protein binding activity of c-Crk
    • Feller S.M., Knudsen B., Hanafusa H. c-Abl kinase regulates the protein binding activity of c-Crk. EMBO J. 13:1994;2341-2351.
    • (1994) EMBO J. , vol.13 , pp. 2341-2351
    • Feller, S.M.1    Knudsen, B.2    Hanafusa, H.3
  • 5
    • 0031669205 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assay for measurement of JNK, ERK and p38 kinase activities
    • Forrer P., Tamaskovic R., Jaussi R. Enzyme-linked immunosorbent assay for measurement of JNK, ERK and p38 kinase activities. Biol. Chem. 379:1998;1101-1111.
    • (1998) Biol. Chem. , vol.379 , pp. 1101-1111
    • Forrer, P.1    Tamaskovic, R.2    Jaussi, R.3
  • 6
    • 0030977270 scopus 로고    scopus 로고
    • MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates
    • Fukunaga R., Hunter T. MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J. 16:1997;1921-1933.
    • (1997) EMBO J. , vol.16 , pp. 1921-1933
    • Fukunaga, R.1    Hunter, T.2
  • 7
    • 0029989229 scopus 로고    scopus 로고
    • Expression of correctly folded proteins in Escherichia coli
    • Georgiou G., Valax P. Expression of correctly folded proteins in Escherichia coli. Curr. Opin. Biotechnol. 7:1996;190-197.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 190-197
    • Georgiou, G.1    Valax, P.2
  • 8
    • 0028905076 scopus 로고
    • Transcription factor ATF2 regulation by the JNK signal transduction pathway
    • Gupta S., Campbell D., Dérijard B., Davis R.J. Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science. 267:1995;389-393.
    • (1995) Science , vol.267 , pp. 389-393
    • Gupta, S.1    Campbell, D.2    Dérijard, B.3    Davis, R.J.4
  • 9
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • Hannig G., Makrides S.C. Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol. 16:1998;54-60.
    • (1998) Trends Biotechnol. , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 10
    • 0028609209 scopus 로고
    • JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation
    • Kallunki T., Su B., Tsigelny I., Sluss H.K., Dérijard B., Moore G., Davis R.J., Karin M. JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev. 8:1994;2996-3007.
    • (1994) Genes Dev. , vol.8 , pp. 2996-3007
    • Kallunki, T.1    Su, B.2    Tsigelny, I.3    Sluss, H.K.4    Dérijard, B.5    Moore, G.6    Davis, R.J.7    Karin, M.8
  • 11
    • 0030693932 scopus 로고    scopus 로고
    • Expression systems: Gene expression systems in the genomic era
    • Kost T.A. Expression systems: Gene expression systems in the genomic era. Curr. Opin. Biotechnol. 8:1997;539-541.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 539-541
    • Kost, T.A.1
  • 13
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • LaVallie E.R., DiBlasio E.A., Kovacic S., Grant K.L., Schendel P.F., McCoy J.M. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Bio/Technology. 11:1993;187-193.
    • (1993) Bio/Technology , vol.11 , pp. 187-193
    • Lavallie, E.R.1    Diblasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 14
    • 0028825817 scopus 로고
    • Gene fusion expression systems in Escherichia coli
    • LaVallie E.R., McCoy J.M. Gene fusion expression systems in Escherichia coli. Curr. Opin. Biotechnol. 6:1995;501-506.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 501-506
    • Lavallie, E.R.1    McCoy, J.M.2
  • 16
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60:1996;512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 17
    • 0026742863 scopus 로고
    • A selective lambda phage cloning vector with automatic excision of the insert in a plasmid
    • Maruyama I.N., Brenner S. A selective lambda phage cloning vector with automatic excision of the insert in a plasmid. Gene. 120:1992;135-141.
    • (1992) Gene , vol.120 , pp. 135-141
    • Maruyama, I.N.1    Brenner, S.2
  • 18
    • 0028168581 scopus 로고
    • Lambda foo: A lambda phage vector for the expression of foreign proteins
    • Maruyama I.N., Maruyama H.I., Brenner S. Lambda foo: a lambda phage vector for the expression of foreign proteins. Proc. Natl. Acad. Sci. USA. 91:1994;8273-8277.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8273-8277
    • Maruyama, I.N.1    Maruyama, H.I.2    Brenner, S.3
  • 19
    • 0030582396 scopus 로고    scopus 로고
    • Surface display of proteins on bacteriophage lambda heads
    • Mikawa Y.G., Maruyama I.N., Brenner S. Surface display of proteins on bacteriophage lambda heads. J. Mol. Biol. 262:1996;21-30.
    • (1996) J. Mol. Biol. , vol.262 , pp. 21-30
    • Mikawa, Y.G.1    Maruyama, I.N.2    Brenner, S.3
  • 20
    • 0030110770 scopus 로고    scopus 로고
    • Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli
    • Murby M., Uhlén M., Ståhl S. Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli. Prot. Expr. Purif. 7:1996;129-136.
    • (1996) Prot. Expr. Purif. , vol.7 , pp. 129-136
    • Murby, M.1    Uhlén, M.2    Ståhl, S.3
  • 21
    • 0032005026 scopus 로고    scopus 로고
    • Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms
    • Netzer W.J., Hartl F.U. Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. Trends Biochem. Sci. 23:1998;68-73.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 68-73
    • Netzer, W.J.1    Hartl, F.U.2
  • 22
    • 0029839322 scopus 로고    scopus 로고
    • Phage display of intact domains at high copy number: A system based on SOC, the small outer capsid protein of bacteriophage T4
    • Ren Z.J., Lewis G.K., Wingfield P.T., Locke E.G., Steven A.C., Black L.W. Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4. Prot. Sci. 5:1996;1833-1843.
    • (1996) Prot. Sci. , vol.5 , pp. 1833-1843
    • Ren, Z.J.1    Lewis, G.K.2    Wingfield, P.T.3    Locke, E.G.4    Steven, A.C.5    Black, L.W.6
  • 24
    • 0025351553 scopus 로고
    • Enhanced translational efficiency with two-cistron expression system
    • Schoner B.E., Belagaje R.M., Schoner R.G. Enhanced translational efficiency with two-cistron expression system. Meth. Enzymol. 185:1990;94-103.
    • (1990) Meth. Enzymol. , vol.185 , pp. 94-103
    • Schoner, B.E.1    Belagaje, R.M.2    Schoner, R.G.3
  • 25
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D.B., Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 67:1988;31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 26
    • 0031045390 scopus 로고    scopus 로고
    • The use of gene fusions to protein A and protein G in immunology and biotechnology
    • Ståhl S., Nygren P.A. The use of gene fusions to protein A and protein G in immunology and biotechnology. Pathol. Biol. Paris. 45:1997;66-76.
    • (1997) Pathol. Biol. Paris , vol.45 , pp. 66-76
    • Ståhl, S.1    Nygren, P.A.2
  • 27
    • 0028907327 scopus 로고
    • Display of peptides and proteins on the surface of bacteriophage lambda
    • Sternberg N., Hoess R.H. Display of peptides and proteins on the surface of bacteriophage lambda. Proc. Natl. Acad. Sci. USA. 92:1995;1609-1613.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1609-1613
    • Sternberg, N.1    Hoess, R.H.2
  • 28
    • 0030842771 scopus 로고    scopus 로고
    • Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor and functionally secreted into the periplasm of Escherichia coli
    • Tudyka T., Skerra A. Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor and functionally secreted into the periplasm of Escherichia coli. Prot. Sci. 6:1997;2180-2187.
    • (1997) Prot. Sci. , vol.6 , pp. 2180-2187
    • Tudyka, T.1    Skerra, A.2
  • 29
    • 0025365143 scopus 로고
    • Gene fusions for purpose of expression: An introduction
    • Uhlén M., Moks T. Gene fusions for purpose of expression: an introduction. Meth. Enzymol. 185:1990;129-143.
    • (1990) Meth. Enzymol. , vol.185 , pp. 129-143
    • Uhlén, M.1    Moks, T.2


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