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Volumn 123, Issue 1, 1998, Pages 30-36

Two-dimensional crystallization of the chaperonin TF55 from the hyperthermophilic archaeon Sulfolobus solfataricus

Author keywords

Chaperonin; Crystallization; Electron microscopy; Image processing; Monolayer

Indexed keywords

CHAPERONIN; PHOSPHOLIPID;

EID: 0032170320     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.4002     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • Amos, L. A., Henderson, R., and Unwin, P. N. (1982) Three-dimensional structure determination by electron microscopy of two-dimensional crystals, Prog. Biophys. Mol. Biol. 39, 183-231.
    • (1982) Prog. Biophys. Mol. Biol. , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.3
  • 2
    • 0030031369 scopus 로고    scopus 로고
    • Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyrus kandleri
    • Andra, S., Frey, G., Nitsch, M., Baumeister, W., and Stetter, K. O. (1996) Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyrus kandleri, FEBS Lett. 379, 127-31.
    • (1996) FEBS Lett. , vol.379 , pp. 127-131
    • Andra, S.1    Frey, G.2    Nitsch, M.3    Baumeister, W.4    Stetter, K.O.5
  • 3
    • 0027956998 scopus 로고
    • Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography
    • Brisson, A., Olofsson, A., Ringler, P., Schmutz, M., and Stoylova, S. (1994) Two-dimensional crystallization of proteins on planar lipid films and structure determination by electron crystallography, Biol. Cell 80, 221-228.
    • (1994) Biol. Cell , vol.80 , pp. 221-228
    • Brisson, A.1    Olofsson, A.2    Ringler, P.3    Schmutz, M.4    Stoylova, S.5
  • 4
    • 0002617993 scopus 로고    scopus 로고
    • A simple model of chaperonin-mediated protein folding
    • Chan, H. S., and Dill, K. A. (1996) A simple model of chaperonin-mediated protein folding, Proteins 24, 345-351.
    • (1996) Proteins , vol.24 , pp. 345-351
    • Chan, H.S.1    Dill, K.A.2
  • 5
    • 0030334841 scopus 로고    scopus 로고
    • Kinetic significance of GroEL(14)center-dot(GroES(7))(2) complexes in molecular chaperone activity
    • Corrales, F. J., and Fersht, A. R. (1996) Kinetic significance of GroEL(14)center-dot(GroES(7))(2) complexes in molecular chaperone activity, Folding Design 1, 265-273.
    • (1996) Folding Design , vol.1 , pp. 265-273
    • Corrales, F.J.1    Fersht, A.R.2
  • 8
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel, L., Löwe, J., Stock, D., Stetter, K-O., Huber, H., Huber, R., and Steinbacher, S. (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT, Cell 93, 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Löwe, J.2    Stock, D.3    Stetter, K.-O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 9
    • 0030907485 scopus 로고    scopus 로고
    • Staphylococcus aureus alpha-toxin - Characterization of protein/lipid interactions: 2D crystallization on lipid monolayers, and 3D structure
    • Ellis, M. J., Hebert, H., and Thelestam, M. (1997) Staphylococcus aureus alpha-toxin - Characterization of protein/lipid interactions: 2D Crystallization on lipid monolayers, and 3D structure, J. Struct. Biol. 118, 178-188.
    • (1997) J. Struct. Biol. , vol.118 , pp. 178-188
    • Ellis, M.J.1    Hebert, H.2    Thelestam, M.3
  • 10
    • 0027920032 scopus 로고
    • Protein folding: Chaperonin duet
    • Ellis, R. J. (1993) Protein folding: Chaperonin duet, Nature 366, 213-214.
    • (1993) Nature , vol.366 , pp. 213-214
    • Ellis, R.J.1
  • 11
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Ellis, R. J., and Hartl, F. U. (1996) Protein folding in the cell: Competing models of chaperonin function, FASEB J. 10, 20-26.
    • (1996) FASEB J. , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 12
    • 0030090632 scopus 로고    scopus 로고
    • Putting a lid on protein folding: Structure and function of the cochaperonin, GroES
    • Fenton, W. A., Weissman, J. S., and Horwich, A. L. (1996) Putting a lid on protein folding: Structure and function of the cochaperonin, GroES, Chem. Biol. 3, 157-161.
    • (1996) Chem. Biol. , vol.3 , pp. 157-161
    • Fenton, W.A.1    Weissman, J.S.2    Horwich, A.L.3
  • 13
    • 0015207572 scopus 로고
    • A new technique for investigating lipid protein films
    • Fromherz, P. (1971) A new technique for investigating lipid protein films, Biochim. Biophys. Acta 225, 382-387.
    • (1971) Biochim. Biophys. Acta , vol.225 , pp. 382-387
    • Fromherz, P.1
  • 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. (1992) Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits, EMBO J. 11, 4767-4778.
    • (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
    • 0028019612 scopus 로고
    • The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro
    • Guagliardi, A., Cerchia, L., Bartolucci, S., and Rossi, M. (1994) The chaperonin from the archaeon Sulfolobus solfataricus promotes correct refolding and prevents thermal denaturation in vitro, Protein Sci. 3, 1436-1443.
    • (1994) Protein Sci. , vol.3 , pp. 1436-1443
    • Guagliardi, A.1    Cerchia, L.2    Bartolucci, S.3    Rossi, M.4
  • 16
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. (1996) Molecular chaperones in cellular protein folding, Nature 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 17
    • 0039507411 scopus 로고
    • Structure of the purple membrane from Halobacterium halobium: Recording, measurement and evaluation of micrographs at 3.5 Å
    • Henderson, R., Baldwin, J. M., Downing, K. H., Lepault, J., and Zemlin, F. (1986) Structure of the purple membrane from Halobacterium halobium: Recording, measurement and evaluation of micrographs at 3.5 Å, Ultramicroscopy 19, 147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 18
    • 0030668929 scopus 로고    scopus 로고
    • Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
    • Klumpp, M., Baumeister, W., and Essen, L. O. (1997) Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin, Cell 91, 263-270.
    • (1997) Cell , vol.91 , pp. 263-270
    • Klumpp, M.1    Baumeister, W.2    Essen, L.O.3
  • 19
    • 0028116350 scopus 로고
    • The molecular chaperonin TF55 from the thermophilic archaeon Sulfolobus solfataricus: A biochemical and structural characterization
    • Knapp, S., Schmidt-Krey, I., Hebert, H., Bergman, T., Jornvall, H., and Ladenstein, R. (1994) The molecular chaperonin TF55 from the thermophilic archaeon Sulfolobus solfataricus: A biochemical and structural characterization, J. Mol. Biol. 242, 397-407.
    • (1994) J. Mol. Biol. , vol.242 , pp. 397-407
    • Knapp, S.1    Schmidt-Krey, I.2    Hebert, H.3    Bergman, T.4    Jornvall, H.5    Ladenstein, R.6
  • 22
    • 0026506038 scopus 로고
    • Two-dimensional crystallization of membrane proteins
    • Kühlbrandt, W. (1992) Two-dimensional crystallization of membrane proteins, Q. Rev. Biophys. 25, 1-49.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 1-49
    • Kühlbrandt, W.1
  • 23
    • 0026683609 scopus 로고
    • T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
    • Lewis, V. A., Hynes, G. M., Zheng, D., Saibil, H., and Willison, K. (1992) T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol, Nature 358, 249-252.
    • (1992) Nature , vol.358 , pp. 249-252
    • Lewis, V.A.1    Hynes, G.M.2    Zheng, D.3    Saibil, H.4    Willison, K.5
  • 25
    • 0031582064 scopus 로고    scopus 로고
    • The thermosome-alternating alpha and beta-subunits within the chaperonin of the archaeon Thermoplasma acidophilum
    • Nitsch, M., Klumpp, M., Lupas, A., and Baumeister, W. (1997) The thermosome-alternating alpha and beta-subunits within the chaperonin of the archaeon Thermoplasma acidophilum, J. Mol. Biol. 267, 142-149.
    • (1997) J. Mol. Biol. , vol.267 , pp. 142-149
    • Nitsch, M.1    Klumpp, M.2    Lupas, A.3    Baumeister, W.4
  • 26
    • 0025892424 scopus 로고
    • A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria
    • Phipps, B. M., Hoffmann, A., Stetter, K. O., and Baumeister, W. (1991) A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria, EMBO J. 10, 1711-1722.
    • (1991) EMBO J. , Issue.10 , pp. 1711-1722
    • Phipps, B.M.1    Hoffmann, A.2    Stetter, K.O.3    Baumeister, W.4
  • 27
    • 0030903748 scopus 로고    scopus 로고
    • Evidence for a lipochaperonin association of active protein-folding GroES oligomers with lipids can stabilize membranes under heat shock conditions
    • Török, Z., Horvath, I., Goloubinoff, P., Kovacs, E., Glatz, A., Balogh, G., and Vigh, L. (1997) Evidence for a lipochaperonin association of active protein-folding GroES oligomers with lipids can stabilize membranes under heat shock conditions, Proc. Natl. Acad. Sci. USA 94, 2192-2197.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2192-2197
    • Török, Z.1    Horvath, I.2    Goloubinoff, P.3    Kovacs, E.4    Glatz, A.B.G.5    Vigh, L.6
  • 28
    • 0029920131 scopus 로고    scopus 로고
    • A review of acquired thermotolerance, heatshock proteins, and molecular chaperones in archaea
    • Trent, J. D. (1996) A review of acquired thermotolerance, heatshock proteins, and molecular chaperones in archaea, FEMS Microbiol Rev. 18, 249-258.
    • (1996) FEMS Microbiol Rev. , vol.18 , pp. 249-258
    • Trent, J.D.1
  • 30
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • Trent, J. D., Nimmesgern, E., Wall, J. S., Hartl, F. U., and Horwich, A. L. (1991) A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1, Nature 354, 490-493.
    • (1991) Nature , vol.354 , pp. 490-493
    • Trent, J.D.1    Nimmesgern, E.2    Wall, J.S.3    Hartl, F.U.4    Horwich, A.L.5
  • 31
    • 0027988048 scopus 로고
    • The essential yeast Tcp1 protein affects actin and microtubules
    • Ursic, D., Sedbrook, J. C., Himmel, K. L., and Culbertson, M. R. (1994) The essential yeast Tcp1 protein affects actin and microtubules, Mol. Biol. Cell 5, 1065-1080.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1065-1080
    • Ursic, D.1    Sedbrook, J.C.2    Himmel, K.L.3    Culbertson, M.R.4
  • 34
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains archaea, bacteria, and eucarya
    • Woese, C. R., Kandler, O., and Wheelis, M. L. (1990) Towards a natural system of organisms: Proposal for the domains archaea, bacteria, and eucarya, Proc. Natl. Acad. Sci. USA 87, 4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3


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