메뉴 건너뛰기




Volumn 62, Issue 1, 1996, Pages 55-60

Combined effects of the signal sequence and the major chaperone proteins on the export of human cytokines in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; HYBRID PROTEIN; INTERLEUKIN 13; SIGNAL PEPTIDE;

EID: 0030023780     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.62.1.55-60.1996     Document Type: Article
Times cited : (39)

References (29)
  • 1
    • 0025976271 scopus 로고
    • Heat-shock proteins can substitute for SecB function during protein export in E. coli
    • Altman, E., C. A. Kumamoto, and S. D. Emr. 1991. Heat-shock proteins can substitute for SecB function during protein export in E. coli. EMBO J. 10:239-245.
    • (1991) EMBO J. , vol.10 , pp. 239-245
    • Altman, E.1    Kumamoto, C.A.2    Emr, S.D.3
  • 3
    • 0028028387 scopus 로고
    • Building bridges: Disulphide bond formation in the cell
    • Bardwell, J. C. A. 1994. Building bridges: disulphide bond formation in the cell. Mill. Microbiol. 14:199-205.
    • (1994) Mill. Microbiol. , vol.14 , pp. 199-205
    • Bardwell, J.C.A.1
  • 4
    • 0026568947 scopus 로고
    • DnaK-mediated alterations in human growth hormone protein inclusion bodies
    • Blum, P., M. Velligan, N. Lin, and A. Matin. 1992. DnaK-mediated alterations in human growth hormone protein inclusion bodies. Bio/Technology 10:301-304.
    • (1992) Bio/Technology , vol.10 , pp. 301-304
    • Blum, P.1    Velligan, M.2    Lin, N.3    Matin, A.4
  • 6
    • 0027975979 scopus 로고
    • Intra- And extracellular expression of an scFv antibody fragment in E. coli: Effect of bacterial strains and pathway engineering using GroES/L chaperonins
    • Duenas M., J. Vasquez, M. Ayala, E. Soderlind, M. Ohlin, L. Pérez, C. A. K. Borrebaeck, and J. V. Gavilondo. 1994. Intra- and extracellular expression of an scFv antibody fragment in E. coli: effect of bacterial strains and pathway engineering using GroES/L chaperonins. BioTechniques 16:476-483.
    • (1994) BioTechniques , vol.16 , pp. 476-483
    • Duenas, M.1    Vasquez, J.2    Ayala, M.3    Soderlind, E.4    Ohlin, M.5    Pérez, L.6    Borrebaeck, C.A.K.7    Gavilondo, J.V.8
  • 7
    • 0022613101 scopus 로고
    • Suppression of the E. coli dnaA46 mutation by amplification of the groES and groEL genes
    • Fayet, O., J. M. Louarn, and C. Georgopoulos. 1986. Suppression of the E. coli dnaA46 mutation by amplification of the groES and groEL genes. Mol. Gen. Genet. 202:435-445.
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 435-445
    • Fayet, O.1    Louarn, J.M.2    Georgopoulos, C.3
  • 8
    • 0026025966 scopus 로고
    • A kinetic partitioning model of selective binding of normative proteins by the bacterial chaperone SecB
    • Hardy, S. J. S., and L. L. Randall, 1991. A kinetic partitioning model of selective binding of normative proteins by the bacterial chaperone SecB. Science 251:439-443.
    • (1991) Science , vol.251 , pp. 439-443
    • Hardy, S.J.S.1    Randall, L.L.2
  • 9
    • 0003694904 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1988. Antibodies. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1988) Antibodies
    • Harlow, E.1    Lane, D.2
  • 10
    • 0026773208 scopus 로고
    • Protein folding in the cell: The role of molecular chaperones Hsp70 and Hsp60
    • Hartl, F. H., J. Martin, and W. Neupert. 1992. Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. Annu. Rev. Biophys. Biomol. Struct. 21:293-322.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 293-322
    • Hartl, F.H.1    Martin, J.2    Neupert, W.3
  • 11
    • 0028128453 scopus 로고
    • Signal peptides: Exquisitely designed transport promoters
    • Izard, J. W., and D. A. Kendall. 1994. Signal peptides: exquisitely designed transport promoters. Mol. Microbiol. 13:765-773.
    • (1994) Mol. Microbiol. , vol.13 , pp. 765-773
    • Izard, J.W.1    Kendall, D.A.2
  • 13
    • 0025303732 scopus 로고
    • Human recombinant interleukin-1B isolated from Escherichia coli by simple osmotic shock
    • Joseph-Liauzun, E., P. Leplatois, R. Legoux, V. Guerveno, E. Marchese, and P. Ferrara. 1990. Human recombinant interleukin-1B isolated from Escherichia coli by simple osmotic shock. Gene 86:291-295.
    • (1990) Gene , vol.86 , pp. 291-295
    • Joseph-Liauzun, E.1    Leplatois, P.2    Legoux, R.3    Guerveno, V.4    Marchese, E.5    Ferrara, P.6
  • 14
    • 0343939593 scopus 로고
    • Escherichia coli SecB protein associates with exported protein precursors in vivo
    • Kumamoto, C. A. 1989. Escherichia coli SecB protein associates with exported protein precursors in vivo. Proc. Natl. Acad. Sci. USA 86:53211-5324.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 53211-55324
    • Kumamoto, C.A.1
  • 15
    • 0024461843 scopus 로고
    • Effects of mutations in heat-shock genes groES and groEL on protein export in E. coli
    • Kusukawa, N., T. Yura, C. Ueguchi, Y. Akiyama, and K. lto. 1989. Effects of mutations in heat-shock genes groES and groEL on protein export in E. coli. EMBO J. 8:3517-3521.
    • (1989) EMBO J. , vol.8 , pp. 3517-3521
    • Kusukawa, N.1    Yura, T.2    Ueguchi, C.3    Akiyama, Y.4    Lto, K.5
  • 17
    • 0028955090 scopus 로고
    • Isolation of an IL13 dependent sub-clone of the B9 cell line useful for the estimation of human IL13 bioactivity
    • Labit-Le Bouteiller, C., R. Astruc, A. Minty, p. Ferrara, and J. Lupker. 1995 Isolation of an IL13 dependent sub-clone of the B9 cell line useful for the estimation of human IL13 bioactivity. J. Immunol. Methods 181:29-36.
    • (1995) J. Immunol. Methods , vol.181 , pp. 29-36
    • Labit-Le Bouteiller, C.1    Astruc, R.2    Minty, A.3    Ferrara, P.4    Lupker, J.5
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0026726710 scopus 로고
    • Effect of overproduction of heat-shock chaperones GroESL and DnaK on human procollagenase production in E. coli
    • Lee, S. C., and P. O. Olins. 1992. Effect of overproduction of heat-shock chaperones GroESL and DnaK on human procollagenase production in E. coli. J. Biol. Chem. 5:2849-2852.
    • (1992) J. Biol. Chem. , vol.5 , pp. 2849-2852
    • Lee, S.C.1    Olins, P.O.2
  • 20
  • 22
    • 0027229503 scopus 로고
    • The Escherichia coli heat shock gene htpY: Mutational analysis, cloning, sequencing, and transcriptional regulation
    • Missiakas, D., C. Georgopoulos, and S. Raina, 1993. The Escherichia coli heat shock gene htpY: mutational analysis, cloning, sequencing, and transcriptional regulation. J. Bacteriol. 175:2613-2624.
    • (1993) J. Bacteriol. , vol.175 , pp. 2613-2624
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 23
    • 0025375220 scopus 로고
    • Heal shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli
    • Phillips, G. J., and T. J. Silhavy. 1990. Heal shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli. Nature (London) 344:882-884.
    • (1990) Nature (London) , vol.344 , pp. 882-884
    • Phillips, G.J.1    Silhavy, T.J.2
  • 24
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.1
  • 25
    • 0027931639 scopus 로고
    • Translocation gets a push
    • Schekman, R. 1994. Translocation gets a push. Cell 78:911-913.
    • (1994) Cell , vol.78 , pp. 911-913
    • Schekman, R.1
  • 26
    • 0025365656 scopus 로고
    • Bacterial genetics by electric shock
    • Solioz, M., and D. Bienz. 1990. Bacterial genetics by electric shock. Trends Biochem. Sci. 15:175-177.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 175-177
    • Solioz, M.1    Bienz, D.2
  • 27
    • 0025361538 scopus 로고
    • The initiation of translation in E. coli: Apparent base-pairing between the 16S-rRNA and downstream sequence of the mRNA
    • Sprengart, M. L., H. P. Fatscher, and E. Fuchs. 1990. The initiation of translation in E. coli: apparent base-pairing between the 16S-rRNA and downstream sequence of the mRNA. Nucleic Acids Res. 18:1719-1723.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1719-1723
    • Sprengart, M.L.1    Fatscher, H.P.2    Fuchs, E.3
  • 28
    • 2642634461 scopus 로고
    • Purified SecB protein of E. coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro
    • Weiss, J. B., P. H. Ray, p. J. Bassford, Jr. 1988. Purified SecB protein of E. coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro. Proc. Natl. Acad. Sci. USA 85:8978-8982.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8978-8982
    • Weiss, J.B.1    Ray, P.H.2    Bassford Jr., P.J.3
  • 29
    • 0026644011 scopus 로고
    • DnaK and DnaJ heat-shock proteins participate in protein export in E. coli
    • Wild, J., E. Altman, T. Yura, and C. C. Gross. 1992 DnaK and DnaJ heat-shock proteins participate in protein export in E. coli. Genes Dev. 6:1165-1172.
    • (1992) Genes Dev. , vol.6 , pp. 1165-1172
    • Wild, J.1    Altman, E.2    Yura, T.3    Gross, C.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.