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Volumn 68, Issue 10, 2004, Pages 2096-2103

GroEL chaperone binding to beetle luciferases and the implications for refolding when co-expressed

Author keywords

DnaK; GroEL; Luciferase; Molecular chaperone; Protein folding

Indexed keywords

BIOLUMINESCENCE; ESCHERICHIA COLI; GENES; SUBSTRATES;

EID: 9244254319     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.68.2096     Document Type: Article
Times cited : (6)

References (26)
  • 1
    • 0029347142 scopus 로고
    • Cloning, expression and sequence analysis of cDNA for the Luciferases from the Japanese fireflies pyrocoelia miyako and Hotaria parvula
    • Ohmiya, Y., Ohba, N., Toh, H., and Tsuji, F. I., Cloning, expression and sequence analysis of cDNA for the Luciferases from the Japanese fireflies pyrocoelia miyako and Hotaria parvula. Photochem. Photobiol., 62, 309-313 (1995).
    • (1995) Photochem. Photobiol. , vol.62 , pp. 309-313
    • Ohmiya, Y.1    Ohba, N.2    Toh, H.3    Tsuji, F.I.4
  • 2
    • 0036865977 scopus 로고    scopus 로고
    • The origin, diversity and structure function relationship of insect luciferases
    • Viviani, V. R., The origin, diversity and structure function relationship of insect luciferases. Cell. Mol. Life Sci., 59, 1833-1850 (2002).
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1833-1850
    • Viviani, V.R.1
  • 3
    • 0033614782 scopus 로고    scopus 로고
    • Cloning, sequence analysis, and expression of active Phrixothrix railroad-worm luciferases: Relationship between bioluminescence spectra and primary structures
    • Viviani, V. R., Bechara, E. J. H., and Ohmiya, Y., Cloning, sequence analysis, and expression of active Phrixothrix railroad-worm luciferases: relationship between bioluminescence spectra and primary structures. Biochemistry, 38, 8271-8279 (1999).
    • (1999) Biochemistry , vol.38 , pp. 8271-8279
    • Viviani, V.R.1    Bechara, E.J.H.2    Ohmiya, Y.3
  • 4
    • 0033547324 scopus 로고    scopus 로고
    • Identification of in vivo substrates of the chaperonin GroEL
    • Houry, W. A., Frishman, D., Eckerskorn, C., Lottspeich, F., and Hartle, F. U., Identification of in vivo substrates of the chaperonin GroEL. Nature, 402, 147-154 (1999).
    • (1999) Nature , vol.402 , pp. 147-154
    • Houry, W.A.1    Frishman, D.2    Eckerskorn, C.3    Lottspeich, F.4    Hartle, F.U.5
  • 5
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartle, F. U., Molecular chaperones in cellular protein folding. Nature, 381, 571-580 (1996).
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartle, F.U.1
  • 6
    • 0041026092 scopus 로고    scopus 로고
    • Interaction of Hsp 70 chaperones with substrates
    • Rudiger, S., Buchberger, A., and Bukau, B., Interaction of Hsp 70 chaperones with substrates. Nature Str. Biol., 4, 342-349 (1997).
    • (1997) Nature Str. Biol. , vol.4 , pp. 342-349
    • Rudiger, S.1    Buchberger, A.2    Bukau, B.3
  • 7
    • 0032541496 scopus 로고    scopus 로고
    • The role of Dnak and HscA homologs of Hsp70 chaperones in protein folding in E. coli
    • Hesterkamp, T., and Bukau, B., The role of Dnak and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J., 17, 4818-4828 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4818-4828
    • Hesterkamp, T.1    Bukau, B.2
  • 8
    • 0034856940 scopus 로고    scopus 로고
    • Chaperone-assisted protein folding in the cell cytoplasm
    • Houry, W. A., Chaperone-assisted protein folding in the cell cytoplasm. Current Protein and Peptide Science, 2, 227-244 (2001).
    • (2001) Current Protein and Peptide Science , vol.2 , pp. 227-244
    • Houry, W.A.1
  • 9
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schroder, H., Langer, T., Hartle, F. U., and Bukau, B., DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J., 12, 4137-4144 (1993).
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schroder, H.1    Langer, T.2    Hartle, F.U.3    Bukau, B.4
  • 10
    • 0032983520 scopus 로고    scopus 로고
    • Co-translations domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • Frydman, J., Bromae, H. E., Tempst, P., and Hartle, F. U., Co-translations domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nature Str. Biol., 6, 697-705 (1999).
    • (1999) Nature Str. Biol. , vol.6 , pp. 697-705
    • Frydman, J.1    Bromae, H.E.2    Tempst, P.3    Hartle, F.U.4
  • 11
    • 0028094779 scopus 로고
    • Folding of firefly luciferase during translation in a cell-free system
    • Kolb, V. A., Makeyev, E. V., and Spirin, A. S., Folding of firefly luciferase during translation in a cell-free system. EMBO J., 13, 3631-3637 (1994).
    • (1994) EMBO J. , vol.13 , pp. 3631-3637
    • Kolb, V.A.1    Makeyev, E.V.2    Spirin, A.S.3
  • 12
    • 0032485847 scopus 로고    scopus 로고
    • Folding of firefly (Photinus pyralis) luciferase: Aggregation and reactivation of unfolding intermediates
    • Herbst, R., Gast, K., and Seckler, R., Folding of firefly (Photinus pyralis) luciferase: Aggregation and reactivation of unfolding intermediates. Biochemistry, 37, 6586-6597 (1998).
    • (1998) Biochemistry , vol.37 , pp. 6586-6597
    • Herbst, R.1    Gast, K.2    Seckler, R.3
  • 13
    • 0030972005 scopus 로고    scopus 로고
    • Equilibrium intermediates in the reversible unfolding of firefly (photinus pyralis) luciferase
    • Herbst, R., Schafer, U., and Seckler, R., Equilibrium intermediates in the reversible unfolding of firefly (photinus pyralis) luciferase. J. Biol. Chem., 272, 7099-7105 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 7099-7105
    • Herbst, R.1    Schafer, U.2    Seckler, R.3
  • 14
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J. S., Tempst, P., and Hartl, F. U., Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J., 11, 4767-4778 (1992).
    • (1992) EMBO J. , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.U.6
  • 15
    • 0027157482 scopus 로고
    • GroE-mediated folding of bacterial luciferase in vivo
    • Escher, A., and Szalay, A. A., GroE-mediated folding of bacterial luciferase in vivo. Mol. Gen. Genet., 238, 65-73 (1993).
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 65-73
    • Escher, A.1    Szalay, A.A.2
  • 16
    • 0031574908 scopus 로고    scopus 로고
    • GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein
    • Fedorov, A. N., and Baldwin, T. O., GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein. J. Mol. Biol., 268, 712-723 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 712-723
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 17
    • 0034050548 scopus 로고    scopus 로고
    • Over expression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli
    • Nishihara, K., Kanemori, M., Yanagai, H., and Yura, T., Over expression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl. Environ. Microbiol., 66, 884-889 (2000).
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 884-889
    • Nishihara, K.1    Kanemori, M.2    Yanagai, H.3    Yura, T.4
  • 18
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone co-expression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen Cryj2 in Escherichia coli
    • Nishihara, K., Kanemori, M., Kitagawa, M., Yanagai, H., and Yura, T., Chaperone co-expression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen Cryj2 in Escherichia coli. Appl. Environ. Microbiol., 64, 1694-1699 (1998).
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagai, H.4    Yura, T.5
  • 19
    • 0035985128 scopus 로고    scopus 로고
    • Co-over expression of folding modulators improves the solubility of the recombinant guinea pig liver trans glutaminase expressed in Escherichia coli
    • Ikura, K., Kokubu, T., Natsuka, S., Ichikawa, A., Adachi, M., Nishihara, A., Yanagi, H., and Utsumi, S., Co-over expression of folding modulators improves the solubility of the recombinant guinea pig liver trans glutaminase expressed in Escherichia coli. Prop. Biochem. Biotechnol., 32, 189-205 (2002).
    • (2002) Prop. Biochem. Biotechnol. , vol.32 , pp. 189-205
    • Ikura, K.1    Kokubu, T.2    Natsuka, S.3    Ichikawa, A.4    Adachi, M.5    Nishihara, A.6    Yanagi, H.7    Utsumi, S.8
  • 20
    • 0020475449 scopus 로고
    • A simple method for displaying hydropathic character of protein
    • Kyte, J., and Doolittle, R. F., A simple method for displaying hydropathic character of protein. J. Mol. Biol., 157, 105-132 (1982).
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 21
    • 9244256644 scopus 로고    scopus 로고
    • The function of chaperones and proteases in protein quality control and intracellular protein degradation
    • ed. Lund, P., Oxford University Press, Oxford
    • Maurizi, M. R., The function of chaperones and proteases in protein quality control and intracellular protein degradation. In "Molecular Chaperones in the Cell", ed. Lund, P., Oxford University Press, Oxford, pp. 205-234 (2001).
    • (2001) Molecular Chaperones in the Cell , pp. 205-234
    • Maurizi, M.R.1
  • 22
    • 0034695615 scopus 로고    scopus 로고
    • GroEL-substrate interactions: Molding the fold, or folding the mold
    • Feltham, J. L., and Gierasch, L. M., GroEL-substrate interactions: molding the fold, or folding the mold. Cell, 100, 193-196 (2000).
    • (2000) Cell , vol.100 , pp. 193-196
    • Feltham, J.L.1    Gierasch, L.M.2
  • 23
    • 0035913910 scopus 로고    scopus 로고
    • GroEL/GroES-mediated folding of a protein too large to be encapsulated
    • Chaudhuri, T. K., Fair, G. W., Fenton, W. A., Rospert, S., and Horwich, A. L., GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell, 107, 235-246 (2001).
    • (2001) Cell , vol.107 , pp. 235-246
    • Chaudhuri, T.K.1    Fair, G.W.2    Fenton, W.A.3    Rospert, S.4    Horwich, A.L.5
  • 24
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a super family of adenylate-forming enzymes
    • Conti, E., Franks, N. P., and Brick, P., Crystal structure of firefly luciferase throws light on a super family of adenylate-forming enzymes. Structure, 4, 287-298 (1996).
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 25
    • 0010350327 scopus 로고    scopus 로고
    • Cell functions of cytosolic E. coli chaperones
    • ed. Lund, P., Oxford University Press, Oxford
    • Mogk, A., Bukau, B., and Deuerling, E., Cell functions of cytosolic E. coli chaperones. In "Molecular Chaperones in the Cell", ed. Lund, P., Oxford University Press, Oxford, pp. 1-34 (2001).
    • (2001) Molecular Chaperones in the Cell , pp. 1-34
    • Mogk, A.1    Bukau, B.2    Deuerling, E.3
  • 26
    • 4544366731 scopus 로고    scopus 로고
    • Improved expression of novel red- and green-emitting luciferases of phrixothrix railroad worms in mammalian cells
    • Nakajima, Y., Kimura, T., Suzuki, C., and Ohmiya, Y., Improved expression of novel red- and green-emitting luciferases of phrixothrix railroad worms in mammalian cells. Biosci. Biotechnol. Biochem., 68, 948-951 (2004).
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 948-951
    • Nakajima, Y.1    Kimura, T.2    Suzuki, C.3    Ohmiya, Y.4


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