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Volumn 262, Issue 2, 1999, Pages 406-416

Purification and characterization of the 16-kda heat-shock-responsive protein from the thermophilic cyanobacterium Synechococcus vulcanus, which is an α-crystallin-related, small heat shock protein

Author keywords

Cyanobacteria; Heat shock protein; Molecular chaperone; Small heat shock protein; Thermophile; crystallin

Indexed keywords

ALPHA CRYSTALLIN; CITRATE SYNTHASE; HEAT SHOCK PROTEIN; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE;

EID: 0033152833     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00380.x     Document Type: Article
Times cited : (56)

References (40)
  • 1
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • 1. Parcell, D.A. & Lindquist, S. (1993) The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27, 437-496.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parcell, D.A.1    Lindquist, S.2
  • 2
    • 0003720391 scopus 로고
    • Progress and perspectives on the biology of heat shock proteins and molecular chaperones
    • (Morimoto, R.I., Tissières, A. & Georgopoulos, C., eds), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • 2. Morimoto, R.I., Tissières, A. & Georgopoulos, C. (1994) Progress and perspectives on the biology of heat shock proteins and molecular chaperones. In The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R.I., Tissières, A. & Georgopoulos, C., eds), pp. 1-30. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 1-30
    • Morimoto, R.I.1    Tissières, A.2    Georgopoulos, C.3
  • 3
    • 0003720391 scopus 로고
    • Expression and function of the low-molecular-weight heat shock proteins
    • (Morimoto, R.I., Tissières, A. & Georgopoulos, C., eds). Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • 3. Arrigo, A.-P. & Landry, J. (1994) Expression and function of the low-molecular-weight heat shock proteins. In The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R.I., Tissières, A. & Georgopoulos, C., eds), pp. 335-373. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.-P.1    Landry, J.2
  • 4
    • 0028284571 scopus 로고
    • Assisting spontaneity, the role of Hsp90 and small Hsps as molecular chaperones
    • 4. Jakob, U. & Buchner, J. (1994) Assisting spontaneity, the role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci. 19, 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 5
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • 5. Waters, E.R., Lee, G.J. & Vierling, E. (1996) Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Bot. 47, 325-338.
    • (1996) J. Exp. Bot. , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 6
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • 6. Boston, R.S., Viitanen, P.V. & Vierling, E. (1996) Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32, 191-222.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 7
  • 8
    • 0024345716 scopus 로고
    • Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells
    • 8. Landry, J., Chretien, P., Lambert, H., Hickey, E. & Weber, L.A. (1989) Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells. J. Cell Biol. 109, 7-15.
    • (1989) J. Cell Biol. , vol.109 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, H.3    Hickey, E.4    Weber, L.A.5
  • 9
    • 0030886055 scopus 로고    scopus 로고
    • Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance
    • 9. Yeh, C.-H., Chang, P.-F.L., Yeh, K.-W., Lin, W.-C., Chen, Y.-M. & Lin, C.-Y. (1997) Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance. Proc. Natl Acad. Sci. USA 94, 10967-10972.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10967-10972
    • Yeh, C.-H.1    Chang, P.-F.L.2    Yeh, K.-W.3    Lin, W.-C.4    Chen, Y.-M.5    Lin, C.-Y.6
  • 10
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • 10. Chang, Z., Primm, T.P., Jakana, J., Lee, I.H., Serysheva, I., Chiu, W., Gilbert, H.F. & Quiocho, F.A. (1996) Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J. Biol. Chem. 271, 7218-7223.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7218-7223
    • Chang, Z.1    Primm, T.P.2    Jakana, J.3    Lee, I.H.4    Serysheva, I.5    Chiu, W.6    Gilbert, H.F.7    Quiocho, F.A.8
  • 11
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • 11. Ehrnsperger, M., Gräber, S., Gaestel, M. & Buchner, J. (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221-229.
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Gräber, S.2    Gaestel, M.3    Buchner, J.4
  • 12
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • 12. Veinger, L., Diamant, S., Buchner, J. & Goloubinoff, P. (1998) The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273, 11032-11037.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 13
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • 13. Lee, G.J., Roseman, A.M., Saibil, H.R. & Vierling, E. (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16, 659-671.
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 14
    • 0024227346 scopus 로고
    • A protein antigen of Mycobacterium leprae is related to a family of small heat shock proteins
    • 14. Nerland, A.H., Mustafa, A.S., Sweetser, D., Godal, T. & Young, R.A. (1988) A protein antigen of Mycobacterium leprae is related to a family of small heat shock proteins. J. Bacteriol. 170, 5919-5921.
    • (1988) J. Bacteriol. , vol.170 , pp. 5919-5921
    • Nerland, A.H.1    Mustafa, A.S.2    Sweetser, D.3    Godal, T.4    Young, R.A.5
  • 15
    • 0026527770 scopus 로고
    • The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is related to the alpha-crystallin family of low-molecular weight heat shock proteins
    • 15. Verbon, A., Hartskeerl, R.A., Schuitema, A., Kolk, A.H.J., Young, D.B. & Lathigra, R. (1992) The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is related to the alpha-crystallin family of low-molecular weight heat shock proteins. J. Bacteriol. 174, 1352-1359.
    • (1992) J. Bacteriol. , vol.174 , pp. 1352-1359
    • Verbon, A.1    Hartskeerl, R.A.2    Schuitema, A.3    Kolk, A.H.J.4    Young, D.B.5    Lathigra, R.6
  • 16
    • 0026784986 scopus 로고
    • Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
    • 16. Allen, S.P., Polazzi, I.O., Gierse, J.K. & Easton, A.M. (1992) Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli. J. Bacteriol. 174, 6938-6947.
    • (1992) J. Bacteriol. , vol.174 , pp. 6938-6947
    • Allen, S.P.1    Polazzi, I.O.2    Gierse, J.K.3    Easton, A.M.4
  • 17
    • 0027465274 scopus 로고
    • Purification and characterization of SP21, a development-specific protein of the myxobacterium Stigmatella aurantiaca
    • 17. Heidelbach, M., Skladny, H. & Schairer, H.U. (1993) Purification and characterization of SP21, a development-specific protein of the myxobacterium Stigmatella aurantiaca. J. Bacteriol. 175, 905-908.
    • (1993) J. Bacteriol. , vol.175 , pp. 905-908
    • Heidelbach, M.1    Skladny, H.2    Schairer, H.U.3
  • 18
    • 0027433255 scopus 로고
    • Heat shock and development induce synthesis of a low-molecular-weight stress-responsive protein in the myxobacterium Stigmatella aurantiaca
    • 18. Heidelbach, M., Skladny, H. & Schairer, H.U. (1993) Heat shock and development induce synthesis of a low-molecular-weight stress-responsive protein in the myxobacterium Stigmatella aurantiaca. J. Bacteriol. 175, 7479-7482.
    • (1993) J. Bacteriol. , vol.175 , pp. 7479-7482
    • Heidelbach, M.1    Skladny, H.2    Schairer, H.U.3
  • 19
    • 0027252458 scopus 로고
    • Sequence and molecular characterization of a DNA region encoding a small heat shock protein of Clostridium acetobutylicum
    • 19. Sauer, U. & Dürre, P. (1993) Sequence and molecular characterization of a DNA region encoding a small heat shock protein of Clostridium acetobutylicum. J. Bacteriol. 175, 3394-3400.
    • (1993) J. Bacteriol. , vol.175 , pp. 3394-3400
    • Sauer, U.1    Dürre, P.2
  • 20
    • 0029074488 scopus 로고
    • Characterization of Streptomyces albus 18-kilodalton heat shock-responsive protein
    • 20. Servant, P. & Mazodier, P. (1995) Characterization of Streptomyces albus 18-kilodalton heat shock-responsive protein. J. Bacteriol. 177, 2998-3003.
    • (1995) J. Bacteriol. , vol.177 , pp. 2998-3003
    • Servant, P.1    Mazodier, P.2
  • 22
    • 0031858563 scopus 로고    scopus 로고
    • Cloning, characterization, and transcriptional analysis of a gene encoding an α-crystallin-related, small heat shock protein from the thermophilic cyanobacterium Synechococcus vulcanus
    • 22. Roy, S.K. & Nakamoto, H. (1998) Cloning, characterization, and transcriptional analysis of a gene encoding an α-crystallin-related, small heat shock protein from the thermophilic cyanobacterium Synechococcus vulcanus. J. Bacteriol. 180, 3997-4001.
    • (1998) J. Bacteriol. , vol.180 , pp. 3997-4001
    • Roy, S.K.1    Nakamoto, H.2
  • 23
    • 0013579792 scopus 로고
    • The cyanobacterial heat-shock response and the molecular chaperones
    • (Bryant, D.A., ed.) Kluwer Academic Publishers, Dordrecht, the Netherlands
    • 23. Webb, R. & Sherman, L.A. (1994) The cyanobacterial heat-shock response and the molecular chaperones. In The Molecular Biology of Cyanobacteria (Bryant, D.A., ed.), pp. 751-767. Kluwer Academic Publishers, Dordrecht, the Netherlands.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 751-767
    • Webb, R.1    Sherman, L.A.2
  • 24
    • 0029924864 scopus 로고    scopus 로고
    • Cloning, characterization and functional analysis of groEL-like gene from thermophilic cyanobacterium Synechococcus vulcanus, which does not form an operon with groES
    • 24. Furuki, M., Tanaka, N., Hiyama, T. & Nakamoto, H. (1996) Cloning, characterization and functional analysis of groEL-like gene from thermophilic cyanobacterium Synechococcus vulcanus, which does not form an operon with groES. Biochim. Biophys. Acta 1294, 106-110.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 106-110
    • Furuki, M.1    Tanaka, N.2    Hiyama, T.3    Nakamoto, H.4
  • 25
    • 0031555336 scopus 로고    scopus 로고
    • Cloning, characterization and functional analysis of groESL operon from thermophilic cyanobacterium Synechococcus vulcanus
    • 25. Tanaka, N., Hiyama, T. & Nakamoto, H. (1997) Cloning, characterization and functional analysis of groESL operon from thermophilic cyanobacterium Synechococcus vulcanus. Biochim. Biophys. Acta 1343, 335-348.
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 335-348
    • Tanaka, N.1    Hiyama, T.2    Nakamoto, H.3
  • 26
    • 0000302666 scopus 로고
    • Photosystem I and photosystem II preparations from thermophilic Synechococcus
    • 26. Katoh, S. (1988) Photosystem I and photosystem II preparations from thermophilic Synechococcus. Methods Enzymol. 167, 263-269.
    • (1988) Methods Enzymol. , vol.167 , pp. 263-269
    • Katoh, S.1
  • 27
    • 0018409915 scopus 로고
    • Generic assignments, strain histories and properties of pure cultures of cyanobacteria
    • 27. Rippka, R., Deruelles, J., Waterbury, J.B., Herdman, M. & Stanier, R.Y. (1979) Generic assignments, strain histories and properties of pure cultures of cyanobacteria. J. Gen. Microbiol. 111, 1-61.
    • (1979) J. Gen. Microbiol. , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3    Herdman, M.4    Stanier, R.Y.5
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 29. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • 30. Cleveland, D.W., Fischer, S.G., Kirschner, M.W. & Laemmli, U.K. (1977) Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252, 1102-1106.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 32
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the α-crystallin small heat-shock protein superfamily
    • 32. de Jong, W.W., Caspers, G.-J. & Leunissen, J.A.M. (1998) Genealogy of the α-crystallin small heat-shock protein superfamily. Int. J. Biol. Macromol. 22, 151-162.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • De Jong, W.W.1    Caspers, G.-J.2    Leunissen, J.A.M.3
  • 33
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • 33. Lee, G.J., Pokala, N. & Vierling, E. (1995) Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J. Biol. Chem. 270, 10432-10438.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 35
    • 0032013798 scopus 로고    scopus 로고
    • The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo
    • 35. Suzuki, T.C., Krawitz, D.C. & Vierling, E. (1998) The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo. Plant Physiol. 116, 1151-1161.
    • (1998) Plant Physiol. , vol.116 , pp. 1151-1161
    • Suzuki, T.C.1    Krawitz, D.C.2    Vierling, E.3
  • 36
    • 0028233236 scopus 로고
    • A 21-kDa chloroplast heat shock protein assembles into high molecular weight complexes in vivo and in organelle
    • 36. Chen, Q., Osteryoung, K. & Vierling, E. (1994) A 21-kDa chloroplast heat shock protein assembles into high molecular weight complexes in vivo and in organelle. J. Biol. Chem. 269, 13216-13223.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13216-13223
    • Chen, Q.1    Osteryoung, K.2    Vierling, E.3
  • 37
    • 0028023344 scopus 로고
    • Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology
    • 37. Groene, P.J., Merck, K.B., de Jong, W.W. & Bloemendal, H. (1994) Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. Eur. J. Biochem. 225, 1-19.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 1-19
    • Groene, P.J.1    Merck, K.B.2    De Jong, W.W.3    Bloemendal, H.4
  • 38
    • 0030973550 scopus 로고    scopus 로고
    • Unique structural features of a noble class of small heat shock proteins
    • 38. Leroux, M.R., Ma, B.J., Batelier, G., Melki, R. & Candido, E.P.M. (1997) Unique structural features of a noble class of small heat shock proteins. J. Biol. Chem. 272, 12847-12853.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12847-12853
    • Leroux, M.R.1    Ma, B.J.2    Batelier, G.3    Melki, R.4    Candido, E.P.M.5
  • 39
    • 0032555364 scopus 로고    scopus 로고
    • Caenorhabditis elegant small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity
    • 39. Kokke, B.P.A., Leroux, M.R., Candido, E.P.M., Boelens, W.C. & de Jong, W.W. (1998) Caenorhabditis elegant small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity. FEBS Lett. 433, 228-232.
    • (1998) FEBS Lett. , vol.433 , pp. 228-232
    • Kokke, B.P.A.1    Leroux, M.R.2    Candido, E.P.M.3    Boelens, W.C.4    De Jong, W.W.5
  • 40
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • 40. Jakob, U., Gaestel, M., Engel, K. & Buchner, J. (1993) Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4


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